WO2014079957A1 - Selective inhibition of ethylene signal transduction - Google Patents

Abstract

The invention relates to a peptide, a peptidomimetic, an antibody and/or fragments thereof, an aptamer as well as small molecules, an agent and a method for influencing the ripening process, the senescence process and/or the stress tolerance of plants and/or the fruits thereof by the inhibition of the interaction of the protein EIN2 (Ethylene Insensitive 2) or an orthologous protein thereof with the receptor protein ETR1 (Ethylene Resistant 1) of its isoforms ERS1, ETR2, ERS2, EIN4 or the homologous or orthologous proteins thereof by a compound inhibiting the interaction.

Description

 SELECTIVE INHIBITION OF ETHYLENE SIGNAL TRANSDUCTION

description

The present invention relates to a method for influencing the

 Ripening process, the senescence process and / or the stress tolerance of plants and / or their fruits by inhibiting the interaction of the protein EIN2 (Ethylene Insensitive 2) or an orthologous protein thereof with the

Receptor protein ETR1 (Ethylene resistant 1) or its isoforms ERS1, ETR2, ERS2, EIN4 or homologous or orthologous proteins thereof. The phytohormone ethylene affects numerous plant growth and growth factors

 Development processes. Transcriptome analyzes indicate that approximately 7% of all genes of a plant genome are regulated by ethylene (G. van Zhong, JK Bums, Profiling ethylene regulated gene expression in Arabidopsis thaliana by microarray analysis, Plant Mol. Bio! 53: 117-131, 2003 ). Ethylene can be produced in the plant in all tissues from the amino acid methionine (Yang, NE Hoffman, Ethylene biosynthesis and its regulation in higher plants Annu Rev. Plant Physiol Plant Mol. Biol. 35: 155-189, 1984 GE Schaller, JJ Kieber, Ethylene, CR Somerville, EM Meyerowitz, eds, The Arabidopsis Book, American Society of Plant Biologists, Rockville, MD, 2002, BS Chauhan, Principles of Biochemistry and

Biophysics, Laxmi Publications, p370; 2008), where the rate of synthesis can vary widely depending on the state of development and tissue type or under the influence of stress. In addition to the adaptation of the plant to changing environmental conditions in response to drought, heat, cold, flooding, mechanical irritation, injury or pathogen infection, the phytohormone also controls numerous physiological processes such as cell extension, flower development, leaf fall, apoptosis, senescence and fruit or seed maturation. Of these diverse processes mediated by the phytohormone, the controlled maturation of fruits from an agronomic point of view for organically grown foodstuffs is

most significant process. Likewise, ethylene plays an important role in the flowering time of flowering plants. By suppressing the ethylene formation leaves For example, the flowering time of cut flowers is significantly longer (MS Reid, MJ Wu, Ethylene and Flower Senescence, Plant Growth Regulation 11, 31-43, 1992).

The natural maturation process takes place in the plant through the endogenously formed ethylene in them. However, the maturation process can also be triggered externally by exogenous ethylene supply or delayed by the suppression of natural ethylene production or the perception of ethylene by the plant. The control of ethylene exposure is used, in particular, for the complete ripening or spoilage of harvested fruits during their

Transport and prevent their storage. Since ethylene is also responsible for the withering of flowering plants, particularly cut flowers, control of ethylene exposure or perception of ethylene may also extend the flowering time of these plants. Ethylene exposure is usually controlled by transporting fruit which has not fully matured, as well as its storage and transport at low temperatures and / or under protective gas such as nitrogen or carbon dioxide or its treatment with inhibitors of ethylene formation or perception of ethylene. In this way, fruits and vegetables can be over long distances without complete

Ripening be transported. Just before the sale to the customer or

Consumers are purposefully induced to ripen fruits by treating them with ethylene or ethylene analogs. However, depending on the country of production, production standards and fruit species, this process still results in considerable post-harvest losses of 10 to 30%. This is partly because the suppression of ripening due to low temperatures and

 Inert gas atmosphere is not possible with all fruits. However, even if this is possible, this method is associated with a high energy consumption for transport and storage and correspondingly high costs. This also applies to the transport and storage of cut flowers (environmental aspects in the flower trade, study on climate compatibility of cut flower production, flowers Rosinski;

Documentation from Myclimate; J. van der Hülst, cold chain management for

Cut flowers, www.flowerwatch.com). To examine the effect of a method on the ethylene response of a fruit, the extent of the delay in ripening can be considered first. Also known as a screening system is the determination of the change in the triple response of seedlings shown by them in the presence of ethylene in the dark (P. Guzman, JR Ecker, Exploiting the Triple Response of Arabidopsis To Identify Ethylene-Related Mutants, Plant Cell 2 : 13-523, 1990). When treated with ethylene, there is a thickening and shortening of the hypocotyl, a shortening of the root and a strong curvature of the Apikaihakens. With the help of altered triple responses in mutants, the receptors and other signaling proteins involved in the ethylene signaling chain could also be identified. These findings have already been used to develop further methods for controlling ethylene exposure.

Thus, ethylene biosynthesis in plants can be inhibited, for example, via the inactivation of genes involved in ethylene biosynthesis in transgenic plants (examples of such transgenic plants can be found in NA Kahn, Ethyiene Action in Plants, Springer Berlin, Heidelberg, New York, 2006, Table 8.1 a) on page 168). Ethylene perception can also be inhibited by genetic alterations of the receptors in transgenic plants (examples of such transgenic plants can be found in NA Kahn, Ethyiene Action in Plants, Springer Berlin, Heidelberg, New York, 2006, Table 8.1 b) on pages 168 -169). Another way to inhibit ethylene perception is to use ethylene antagonists. As the first ethylene analogues, which as well as the phytohormone trigger a triple response in seedlings, were propylene, acetylene and

Carbon monoxide as well as alkenes and alkene-related compounds are identified (S.P. Burg, E.A. Burg, Molecular requirement for the biological activity of ethyiene, Plant Physiol 42: 144-152). Later, isocyanides have also been shown to play a role as ethylene antagonists (E.C. Sisler, Ethyiene acitvity of some Tau-acceptor Compounds, Tob Sei 21: 43-45, 1977). Various cyclic alkenes (examples of which can be found in N.A. Kahn, Ethyiene Action in Plants,

Springer Berlin, Heidelberg, New York, 2006, Table 1.1) and naturally occurring terpenes (examples of which can be found in NA Kahn, Ethyiene Action in Plants, Springer Berlin, Heidelberg, New York, 2006, Table 1.2) inhibit the ethylene response and act as ethylene antagonists. Likewise, silver ions such as Silver nitrate, silver sulfate and silver thiosulfate effective ethylene antagonists. Very effective ethylene antagonists are cyclopropenes (examples of which can be found in

N.A. Kahn, Ethylene Action at Plants, Springer Berlin, Heidelberg, New York, 2006, Table 1.3). For example, compound 1-methylcyclopropene (1-MCP) is sold under the trade name Ethylbioc for flowers and Smartfresh for edible products.

However, all of these ethylene antagonists, with the exception of silver sulfate and cyclopropene, have in common that they require continuous application and exposure in order to be effective. The use of some substances like

Norbornadiene or trans-cyciooctene is also associated with a strong odor nuisance. The practical applicability of 1-MCP is limited because it is unstable in liquid form or in solution except at low temperatures, and is stable only in the gaseous state under an inert gas atmosphere. From this fact of application in the gaseous state, however, results that an exposure of the fruit or flowers can only be done in closed, gas-tight rooms. In addition, the water solubility of 1-MCP is insufficient. In addition, the effect of 1-MCP at low temperatures used in the storage and transportation of fruits or flowers is less than at room temperature, so that effectively a larger amount of 1-MCP must be used under conditions of use. In some cases, such as parsley or pears, 1-MCP even speeds up the

Ethylene production and thus has a negative effect on maturation. In

different stone fruits have only a limited effect with 1-MCP and daffodils are even insensitive to 1-MCP. Another way to control ethylene exposure is to inhibit ethylene-induced

Target proteins there. This option is currently only on the inhibition

Cell wall modifying enzymes in transgenic plants limited (examples can be found in N. A. Kahn, Ethylene Action in Plants, Springer Berlin, Heidelberg, New York, 2006, Table 8.1 c) on page 169).

Overall, the control of Ethylenexposition of plants and their fruits as well as of flowering plants is currently a method that is associated in particular with high costs. Thus, the present invention, starting from the prior art in particular the task of providing a method for controlling the maturation process, the senescence process and / or the stress tolerance of plants and / or their fruits to provide, which preferably at least one of the disadvantages discussed above fixes known in the prior art method. In particular, the object of the present invention is to provide a process in which post-harvest losses, that is, post-harvest spoilage of food, in particular before the consumer is reached, are reduced over the processes described in the prior art. In addition, a method is to be provided which preferably provides effective control of the

 Maturation process, the senescence process and / or the stress tolerance to a variety of different plants, fruits and flowering plants has.

At least part of these objects are achieved, preferably all of these objects, by providing a compound selected from the group consisting of a peptide, a peptide mimetic and an aptamer, a means and / or a method for influencing the maturation process, the senescence process and / or the stress tolerance of plants and / or their fruits, as explained in more detail below.

In particular, these tasks are solved by providing a

A compound which is selected from the group consisting of a peptide, a peptide mimetic and an aptamer, characterized in that the peptide consists of an amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 1, the

 Amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, that the

Peptide mimetic consists of a peptide backbone modified amino acid sequence which is selected from the group consisting of

Amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the Amino acid sequence SEQ ID NO: 3, a permutation of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of

 Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3 or that the aptamer is prepared on the basis of the target structure of a peptide, wherein the peptide is selected from the amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3. In this case, compounds are excluded in which the peptide from an amino acid sequence of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 or SEQ ID NO: 102, and / or from a part of one of the amino acid sequences SEQ ID NO: 98 to SEQ ID NO: 102, which comprises at least 6 of the amino acids mentioned in SEQ ID NO: 98 to SEQ ID NO: 102 and / or from a derivative of the amino acid sequences SEQ ID NO: 98 to 102 and / or in which a peptide mimetic consists of an am

 Peptide backbone modified amino acid sequence which is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 102, and / or in which Aptamer is prepared based on the peptide structure of a peptide, wherein the peptide is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100 SEQ ID NO: 101 and SEQ ID NO: 102.

Likewise, these objects are achieved by providing a compound which is selected from the group consisting of a peptide, a

Peptidomimetic an antibody and / or its fragments and an aptamer, characterized in that the peptide and / or the antibody and / or fragments thereof, the amino acid sequence SEQ ID NO: 103, or a part of

Amino acid sequence SEQ ID NO: 103, which at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 103 or comprises a derivative of the amino acid sequence SEQ ID NO: 103 or that the peptide mimetic has the peptide backbone modified amino acid sequence SEQ ID NO: 103 or a portion of the peptide backbone modified amino acid sequence SEQ ID NO: 103, which at least 4, preferably at least 5, especially preferably comprises at least 6 of the amino acids recited in SEQ ID NO: 103, or a derivative of the peptide backbone modified amino acid sequence SEQ ID NO: 103 comprises or the aptamer is prepared based on the target structure of a peptide, wherein the peptide is selected from the amino acid sequence SEQ ID NO: 103, a part of the amino acid sequence SEQ ID NO: 103 which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 103, and a derivative of the amino acid sequence SEQ ID NO: 103, wherein, when the amino acid sequence comprises SEQ ID NO: 103 at one position alanine, none of the other amino acid n of SEQ ID NO: 103 is alanine. Furthermore, these objects are achieved in particular by providing a means for influencing the ripening process, the senescence process and / or the stress tolerance of plants and / or their fruits

at least one compound selected from the group consisting of a peptide, a peptide mimetic, an aptamer, an antibody and / or its fragments, characterized in that the peptide or antibody and / or its fragments comprises an amino acid sequence which is selected is selected from the group consisting of the amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3 that the

Peptide mimetic comprises at least one peptide backbone modified amino acid sequence selected from the group consisting of

 Amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which is at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3 or that the aptamer

Based on the target structure of a peptide is prepared, wherein the peptide is selected from the amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of the

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3 _» and a derivative of one of

 Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3. In this case, compounds are excluded in which the peptide or antibody and / or fragments thereof has an amino acid sequence of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100 , SEQ ID NO: 101 or SEQ ID NO: 102, and / or a part of one of the

Amino acid sequences SEQ ID NO: 98 to SEQ ID NO: 102, which comprises at least 6 of the amino acids mentioned in SEQ ID NO: 98 to SEQ ID NO: 102 and / or comprises a derivative of the amino acid sequences SEQ ID NO: 98 to 102 and / or where a peptide mimetic is modified from one on the peptide backbone

An amino acid sequence is selected which is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 102, and / or in which an aptamer Based on the target structure of a peptide, wherein the peptide is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100 SEQ ID NO: 101 and SEQ ID NO: 102.

Likewise, these objects are achieved in particular by providing a means for influencing the maturation process, the senescence process and / or the stress tolerance of plants and / or their fruits comprising at least one compound which is selected from the group consisting of a peptide, a peptide mimetic, an aptamer, an antibody and / or its

 Fragments, characterized in that the peptide or the antibody and / or its fragments have the amino acid sequence SEQ ID NO: 103, a part of

Amino acid sequence SEQ ID NO: 103, which at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 103 or a derivative of the amino acid sequence SEQ ID NO: 103, the peptide mimetic comprises the peptide backbone modified amino acid sequence SEQ ID NO: 103, a portion of a peptide backbone modified amino acid sequence SEQ ID NO: 103, which is at least 4, preferably at least 5, especially preferably comprises at least 6 of the amino acids recited in SEQ ID NO: 103, or a derivative of a peptide backbone modified amino acid sequence SEQ ID NO: 103 or that the aptamer is prepared based on the target structure of a peptide, wherein the peptide is selected from the amino acid sequence SEQ ID NO: 103, a part of one of the amino acid sequences SEQ ID NO: 103, which

at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 103, and a derivative of the

Amino acid sequence SEQ ID NO: 103, wherein, when the amino acid sequence SEQ ID NO: 103 comprises alanine at one position, none of the other amino acids of SEQ ID NO: 103 is alanine.

Furthermore, these objects are achieved by providing a method for influencing the maturation process, the senescence process and / or the stress tolerance of plants and / or their fruits, characterized in that in the plants and / or fruits, the interaction of the protein EIN2 (Ethylene

Insensitive 2) or an orthologous protein thereof with the receptor protein ETR1 (Ethylene resistant 1), its isoforms E S1, ETR2, ERS2, IN4 or homologous or orthologous proteins thereof by the interaction of a compound, which is selected from the group _'consisting of a Peptide, one

Peptide mimetic, an aptamer, an antibody and / or setner fragments, small molecules and mixtures of these compounds with a contact domain of the ethylene receptor ETR1 or its isoforms ERS1, ETR2, ERS2, EIN4 or a homologous or orthologous protein thereof is inhibited, wherein the contact domain is that which interacts with EIN2 or an orthologous protein thereof and wherein the peptide, the antibody and / or its fragments at least one

Amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which is at least 4, preferably at least 5, more preferably at least 8 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, the peptide mimetic

at least one amino acid sequence modified on the peptide backbone, which is selected from the group consisting of the amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of the amino acid sequences SEQ ID NO 1 to SEQ ID NO: 3, a part of one of the amirosanic acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which contains at least 4, preferably at least 5, particularly preferably at least 6, of SEQ ID NO: 1 to SEQ ID NO: 3 amino acids, and a derivative of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3 or the aptamer based on the target structure of a peptide is prepared, wherein the peptide is selected from the amino acid sequence SEQ ID NO: 1, the Amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3; which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3. In this case, compounds are excluded in which the peptide or antibody and / or fragments thereof has an amino acid sequence of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100 , SEQ ID NO: 101 or SEQ ID NO: 102, and / or a part of one of the

Amino acid sequences SEQ ID NO: 98 to SEQ ID NO: 102, which comprises at least 6 of the amino acids mentioned in SEQ ID NO: 98 to SEQ ID NO: 102 and / or comprises a derivative of the amino acid sequences SEQ ID NO: 98 to 102 and / or where a peptide mimetic is modified from one on the peptide backbone

An amino acid sequence is selected which is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 102, and / or in which an aptamer Based on the target structure of a peptide, wherein the peptide is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100 SEQ ID NO: 101 and SEQ ID NO: Likewise, these objects are achieved by providing a method for influencing the maturation process, the senescence process and / or the stress tolerance of plants and / or their fruits, characterized in that in the plants and / or fruits, the interaction of the protein E1N2 (Ethylene

Insensitive 2) or an orthologous protein thereof with the receptor protein ETR1 (Ethylene resistant 1), its isoforms ERS1, ETR2, ERS2, EIN4 or homologous or orthologous proteins thereof by the interaction of a compound selected from the group consisting of a peptide one

Peptide mimetic, an aptamer, an antibody and / or its fragments, small molecules and mixtures of these compounds with a contact domain of the ethylene receptor ETR1 or its isoforms ERS1, ETR2, ERS2, EIN4 or a homologous or orthologous protein thereof is inhibited, wherein the contact domain is that which interacts with EIN2 or an orthologous protein thereof and wherein the peptide, the antibody and / or its fragments at least one

Amino acid sequence SEQ ID NO: 103, a part of the amino acid sequence SEQ ID NO: 103, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 103, or a derivative of the amino acid sequence SEQ ID NO: 103 the peptide mimetic comprises at least one amino acid sequence modified at the peptide backbone SEQ ID NO: 103, a part of the peptide backbone modified amino acid sequence SEQ ID NO: 103, which at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 103 or a derivative of the peptide backbone modified amino acid sequence of SEQ ID NO: 103 or the aptamer is prepared based on the target structure of a peptide, wherein the peptide is selected from the amino acid sequence SEQ ID NO: 103, a part of

Amino acid sequence SEQ ID NO: 103, which comprises at least 4, preferably at least 5, particularly preferably at least 6, of the amino acids mentioned in SEQ ID NO: 103, and a derivative of the amino acid sequence SEQ ID NO: 103, where if the amino acid sequence SEQ ID NO: 103 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 103 is alanine.

It has surprisingly been found that the compound according to the invention, the agent according to the invention and the process according to the invention are effective in controlling the rearing process, the senescence process and / or the Stress tolerance in a variety of different plants, fruits and

This makes it possible to save considerable energy costs, which arise in particular through the cooling of fruits or else the increased consumption of flowering plants with a shorter flowering time.

For the purposes of the present invention, the term "control of ethylene exposure" is used equivalently for influencing retraction processes, senescence processes and / or stress tolerance of plants and / or their fruits, in which case maturation processes include, in particular, complete suppression and / or

Delay the maturation of plants and / or their fruits. A

 Suppression and / or delay of ripening is particularly present when the plants and / or their fruits at the time of acceptance by the

End consumers, that is, after transport and optionally subsequent storage, not yet spoiled in comparison to the same plant and / or their fruits, which was not treated according to the invention. In relation to

 In particular, flowering plants means that the senescence process is delayed. For the purposes of the present invention is under the delay of

Senescence process in particular the extension of the flowering time of the treated plant according to the invention compared to the same plant, which was not treated according to the invention to understand. Furthermore, "influencing the stress tolerance" as used in the context of the invention preferably means an improved adaptation of the morphological, physiological and biochemical state of the plants and / or their fruits to stress factors, in particular dryness, heat, cold , Flooding, salinity, mechanical irritation, injury or pathogen infection understood.

The term "plant" is used interchangeably in the present invention for the fruits of the plant, and in particular also for flowering plants, In particular, this term includes all aboveground and subterranean parts and organs of the plant, such as shoot, leaf, flower and root, by way of example Leaves, needles, stems, stems, flowers, fruiting bodies, fruits and seeds, as well as roots, tubers and rhizomes As mentioned above, the plant parts also include crops and vegetative and generative propagation material such as cuttings, tubers, rhizomes, cuttings and seeds. The interaction inhibiting compound

In the method according to the invention, the interaction of the protein E1N2 or an orthologous protein with the receptor protein ETR1 or its isoforms ERS1, ETR2, ERS2, EIN4 or a homologous or orthologous protein by a

Compound inhibited which is selected from the group consisting of a peptide, a peptide mimetic, an aptamer, an antibody and / or its fragments, small molecules and mixtures of these compounds. Mixtures of these compounds preferably comprise two of said compounds, but may also comprise more than two of the compounds. The following is the

 A compound which is selected from the group consisting of a peptide, a peptide mimetic, an aptamer, an antibody and / or its

Fragments, small molecules and mixtures of these compounds, also referred to as "the interaction-inhibiting compound".

In a preferred embodiment of the present invention, the term "comprising" means "consisting of".

According to the present invention, the term "peptide" is used in particular for an amino acid sequence of up to 100 amino acids, preferably up to 50 amino acids, most preferably up to 12, more preferably up to 10, most preferably up to 8 amino acids by the term peptides, preferably L-peptides comprising a sequence of L-amino acids.

The term "peptide mimetic" describes a low molecular weight compound whose essential structural elements are modeled on those of a peptide and which can thereby have similar biological activity to peptides, Preferably, the low molecular weight compound has a molecular weight of up to 11000 g / mol.

Particularly preferably, the low molecular weight compound has a molecular weight between 500 to 5000 g / mol, very particularly preferably from 1000 to 1500 g / mol,

Preferably, peptide mimetics include D-peptides which have a sequence of D-

Include amino acids. These are especially designed to have the biological activity of the corresponding natural L-peptides. Further preferably, peptide mimetics include peptides whose backbones are chemically modified. Preferably, these have chemically modified on the backbone Peptides an optionally modified amino acid sequence of up to 100 amino acids, preferably up to 50 amino acids, most preferably up to 12, further preferably up to 10, most preferably up to 8 amino acids on. In this case, the peptide index is particularly preferably replaced by a bioisosteric group. Most preferably, peptide mimetics have an amino acid sequence structure in which at least one of the peptide backbones (* NHCO *) of the peptide backbone is selected by an isosteric group selected from the group consisting of ^* CH ₂ -CH ₂ *. * CO-0 *. * CHOH-CH ₂ *, * CH ₂ -0 *, * CH ₂ -NH *, * CH ₂ -S ^* . * CS-NH * and N- modified * N CO * - is replaced. Likewise, a modification of the peptide backbone may optionally additionally comprise a cyclization. According to the present invention, the term peptide mimetic also includes "peptoids" (N-substituted polyglycine) which have an amino acid sequence structure in which at least one of the peptide bonds ( ^* NHCO ^* ) of the peptide backbone is replaced by an N-modified ^* NRCO * group and where R corresponds to the amino acid side chain which in a corresponding peptide to the a carbon atom

is bound. It is preferred that the peptoids have a

Have amino acid sequence structure corresponding to an amino acid sequence of up to 100 amino acids, preferably up to 50 amino acids, most preferably up to 12, further preferably up to 10, most preferably up to 8 amino acids. Most preferably, peptoids have exclusively a structure analogous to a peptide, in which all peptide bonds are N-modified

* NRCO * groups are replaced and R corresponds in each case to the amino acid side chain which is bound in an analogous peptide to the a-carbon atom. In one embodiment, the peptide mimetic is a peptoid.

The term "aptamer" as used in the context of the invention refers to single- or double-stranded DNA or RNA oligonucleotides, which are characterized in particular in that they can bind specifically to a molecule via their 3D structure They can bind specifically to the contact domain of ETR1 The identification of DNA and RNA aptamers can be done via SELEX (Systematic Evolutton of Ligands by Exponential Enrichment) {C. Tuerk, L. Gold, Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase, Science 249, 505-510; 1990; DW Drolet, RD Jenison, DE Smith, D. Pratt, BJ Hicke, A high throughput platform for systematic evolution of ligands by exponential enrichment (SELEX) Comb. Chem. High Throughput Screen. 2, 271-278 _» ; 1999). The target structure here can preferably be a peptide which is selected from the amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, the amino acid sequence SEQ ID NO: 4, a permutation of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 4, a part of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 4, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 4, and a derivative of one of

 Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 4, are presented. In this case, compounds are excluded in which the peptide from an amino acid sequence of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 or SEQ ID NO: 102, and / or from a part of a the amino acid sequences SEQ ID NO: 98 to SEQ ID NO: 102, which comprises at least 6 of the amino acids mentioned in SEQ ID NO: 98 to SEQ ID NO: 102 and / or from a derivative of the

Amino acid sequences SEQ ID NO: 98 to 102 consists.

In another embodiment, the target structure is a peptide selected from the amino acid sequence SEQ ID NO: 103, a part of

Amino acid sequence SEQ ID NO: 103, which comprises at least 4, preferably at least 5, particularly preferably at least 6, of the amino acids mentioned in SEQ ID NO: 103, and a derivative of the amino acid sequence SEQ ID NO: 103, where if the amino acid sequence SEQ ID NO: 103 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 103 is alanine. The target structure is particularly preferably selected from the group consisting of an amino acid sequence SEQ ID NO: 103, SEQ ID NO: 104, SEQ ID NO: 105, SEQ ID NO: 106, SEQ ID NO: 107, SEQ ID NO: 108, a portion of the amino acid sequence SEQ ID NO: 103, SEQ ID NO: 104, SEQ ID NO: 105, SEQ ID NO: 106, SEQ ID NO: 107, SEQ ID NO: 108, which is at least 4, preferably at least 5, particularly preferred at least 6 of the amino acids mentioned in SEQ ID NO: 103 to SEQ ID NO: 108, and a derivative of one of the amino acid sequence SEQ ID NO: 103, SEQ ID NO: 104, SEQ ID NO: 105, SEQ ID NO: 106, SEQ ID NO: 107 and SEQ ID NO: 108, wherein if one of the amino acid sequences SEQ ID NO: 103, SEQ ID NO: 104, SEQ ID NO: 105, SEQ ID NO: 106, SEQ ID NO: 107 or SEQ ID NO: 108 at one position comprises alanine, none of the other amino acids of the corresponding SEQ ID NO: is alanine. Most preferably, the target structure is one

An amino acid sequence selected from the group consisting of SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 110, SEQ ID NO: 111, SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO: 114, SEQ ID NO: 115, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 118, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124. Also, in H. Kawaki, S. Kubota, E. Aoyama, N. Fujita, H. Hanagata, A. Miyauchi, K. Nakai, M. Takigawa, Desgin and Utility of CCN2 anchor peptide aptamer, Biochimie 92 (2010) 1010-1015 and in CJ Brown et al., Rational design and biophysical characterization of thioredoxin-based aptamer: insights into peptide grafting, J. Mol. Biol. 295 (2012) 871 -883 the

Preparation of aptamers described. Here, too, the abovementioned peptides can be used as the basis for aptamer production.

An "antibody and / or its fragments" refers to a protein and / or its subsequence from the class of globulins Preferably, this monoclonal antibody and / or its fragments is directed against the domain of the EIN2 or an orthologous protein which is in contact with the contact domain of the ETR1 Very particular preference is given to the antibody and / or its fragment based on a peptide which is selected from the amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, the amino acid sequence SEQ ID NO: 4, a permutation of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 4, a part of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 4, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 4, and a derivative of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 4, prepared. In this case, compounds are excluded in which the antibody and / or its fragment has an amino acid sequence of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 or SEQ ID NO: 102, and / or a part of one of

Amino acid sequences SEQ ID NO: 98 to SEQ ID NO: 102, which comprises at least 6 of the amino acids mentioned in SEQ ID NO: 98 to SEQ ID NO: 102 and / or comprises a derivative of the amino acid sequences SEQ ID NO: 98 to 102. In another embodiment, the antibody and / or its fragment is prepared on the basis of a peptide which is selected from the amino acid sequence SEQ ID NO: 103, a part of the amino acid sequence SEQ ID NO: 103, which is at least 4, preferably at least 5, particularly preferred at least 6 of the amino acids mentioned in SEQ ID NO: 103, and a derivative of the

Amino acid sequence SEQ ID NO: 103, wherein, when the amino acid sequence SEQ ID NO: 103 comprises alanine at one position, none of the other amino acids of SEQ ID NO: 103 is alanine. The antibody and / or its fragment are particularly preferably prepared on the basis of a peptide which is selected from the group consisting of an amino acid sequence SEQ ID NO: 103, SEQ ID NO: 104, SEQ ID NO: 105, SEQ ID NO: 106 , SEQ ID NO: 107, SEQ ID NO: 108 part of the

Amino acid sequence SEQ ID NO: 103, SEQ ID NO: 104, SEQ ID NO: 105, SEQ ID NO: 106, SEQ ID NO: 107, SEQ ID NO: 108, which at least 4, preferably at least 5, particularly preferably at least 6 of in SEQ ID NO: 103 to SEQ ID NO: 108, and a derivative of one of the

Amino acid sequences SEQ ID NO: 103, SEQ ID NO: 104, SEQ ID NO: 105, SEQ ID NO: 106 SEQ ID NO: 107 and SEQ ID NO: 108, wherein when one of the

Amino acid sequences SEQ ID NO: 103, SEQ ID NO: 104, SEQ ID NO: 105, SEQ ID NO: 106, SEQ ID NO: 107 or SEQ ID NO: 108 at one position comprises alanine, none of the other amino acids of the corresponding SEQ ID NO: Alanine is.

Most preferably, the antibody and / or its fragment is prepared on the basis of an amino acid sequence which is selected from the group consisting of SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 110, SEQ ID NO: 111 , SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO: 114, SEQ ID NO: 115, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 118, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124.

According to the present invention, "small molecules" are chemical ones

Compounds which are suitable to interact with the contact domain of the ETR1 or a homologous or orthologous protein thereof and have a molecular weight of preferably at most 1500 g / mol. Preferably, small molecules have similar physicochemical properties as the peptide SEQ ID NO: 4. Most preferably, small molecules have similar physicochemical Properties such as a peptide selected from the group consisting of SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 110, SEQ ID NO: 11 1, SEQ ID NO: 1 12, SEQ ID NO: 1 13, SEQ ID NO: 1 14, SEQ ID NO: 1 15, SEQ ID NO: 1 16, SEQ ID NO: 1 17, SEQ ID NO: 118, SEQ ID NO: 1 19, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124. Most preferably, the small molecules have a positive partial charge or charge. Most preferably, the small molecules have a net charge of +3 to +7, most preferably +4 to +6. Also preferably, small molecules have an isoelectric point at 25 ° C of pH = 10 to 14, more preferably from 11 to 13. Further preferred, they have a hydrophobicity of + 12 to + 18 Kcal / mol, more preferably from +13 to +17 Kcal / mol. Most preferably, the small molecules have a net charge of +5. Furthermore, very particularly preferably, the small molecules have an isoelectric point of pH = 12.2. Likewise, most preferably, they have a hydrophobicity of + 15, 7 Kcal / mol.

Those skilled in the methods are known to the above-mentioned effective

Identify connections. Preferably, he can understand the structural and

Electrostatic requirements based on the following homology model can be determined by comparative modeling with the program MODELER 9.11 (A.Sali & TL Blundell, Comparative protein modeling by satisfaction of spatial restraints, J.Mol., Biol., 234, 779-815, 1993) the basis of the crystal structure of the RNA-directed RNA polymerase (RCSB protein data bank: 4f5x.pdb) was created, which has an 87.5 percent match with SEQ ID NO: 4 in the sequence section 160-167 (see also Figure 8):

Table 1: Homology model

 EXPDTA T HEORET ICAL MODE

HELIX 8 8 LY S 2 ARG 7 1 6

 ATOM 1 N LEU 1 335.645 5,917 372,542 0.20 188.39 N

 ATOM 2 H LEU 1 335.545 5,839 373,574 1.00 168.39

 ATOM 3 CA LEU 1 334.308 6.055 371.927 0.20 168.39 C

 ATOM 4 HA LEU 1 334.446 6.100 370.858 1.00 168.39 H

 ATOM 5 CB LEU 1 333.403 4.874 372.313 0.20 168.39 C

ATOM 6 HB3 LEU 1 333.869 3.928 371.961 1.00 168.39 H ATOM 7 HB2 LEU 1 333.314 4.827 373.421 1.00 168.39 H

ATOM 8 CG LEU 1 331.998 5,000 371,686 0.20 168.39

ATOM 9 HG LEU i 331.994 3.888 371.650 1.00 168.39 H

ATOM 10 CD1 LEU! 331,914 4,904 370,156 0.20 168.39 c

ATOM 11 HD11 LEU 1 332.484 4.020 369.802 1.00 168.39 H

ATOM 12 HD12 LEU! 332,345 5,816 369,692 1.00 168.39 H

ATOM 13 HD13 LEU 1 330.857 4.801 369.834 1.00 168.39 H

ATOM 14 CD2 LEU 1 330.776 4.753 372.583 0.20 168.39 c

ATOM 15 HD21 LEU 1 331.025 4.040 373.397 1.00 168.39 H

ATOM 16 HD22 LEU! 330,430 5,708 373,035 1.00 168.39 H

ATOM 17 HD23 LEU 1 329.945 4.327 371.979 1.00 168.39 H

ATOM 18 C LEU 1 333.646 7.305 372.394 0.20 168.39 C

ATOM 19 O LEU 1 333.063 8.040 371.603 0.20 168.39 O

ATOM 20 H2 LEU 1 336.112 5.063 372.174 1.00 168.39 H

ATOM 21 H3 LEU 1 336.218 6.752 372.310 1.00 168.39 H

! ATOM 22 N LYS 2 333.734 7.576 373.708 0.20 101.11 N

ATOM 23 H LYS 2 334.221 6.977 374.340 1.00 101.11 H

ATOM 24 CA LYS 2 333.097 8.723 374.282 0.20 101.11 C

ATOM 25 HA LYS 2 332.038 8.658 374.081 1.00 101.11 H

ATOM 26 CB LYS 2 333.381 8,818 375.791 0.20 101.11 C

ATOM 27 HB3 LYS 2 334.482 8.833 375.934 1.00 101.11 H

ATOM 28 HB2 LYS 2 332.964 9.763 376.200 1.00 101.11 H

ATOM 29 CG LYS 2 332.806 7.638 376.582 0.20 101.11 C

ATOM 30 HG3 LYS 2 333.070 6.697 376.052 1.00 101.11 H

ATOM 31 HG2 LYS 2 331.698 7.721 376.608 1.00 101.11 H

ATOM 32 CD LYS 2 333.351 7.533 378.012 0.20 101.11 C

ATOM 33 HD3 LYS 2 334.440 7.321 377.968 1.00 101.11 H

ATOM 34 HD2 LYS 2 332.852 6.679 378.515 1.00 101.11 H

ATOM 35 CE LYS 2 333.140 8.797 378.851 0.20 101.11 C

ATOM 36 HE3 LYS 2 333.676 9.663 378.404 1.00 101.11

ATOM 37 HE2 LYS 2 333.503 8.641 379.890 1.00 101.11 H

ATOM 38 NZ LYS 2 331.702 9.130 378.918 0.20 101.11 N

ATOM 39 HZ1 LYS 2 331.571 9,998 379,478 1.00 101.11 H

ATOM 40 HZ2 LYS 2 331.344 9.283 377.954 1.00 101.11 H

ATOM 41 HZ3 LYS 2 331.182 8.348 379.363 1.00 101.11 H

ATOM 42 C LYS 2 333.654 9.957 373.642 0.20 101.11 C

ATOM 43 o LYS 2 332.907 10.831 373.203 0.20 101.11 O

ATOM 44 N ARG 3 334.991 10.049 373.552 0.20 999.99 N

ATOM 45 H ARG 3 335.601 9.332 373.882 1.00 999.99

ATOM 46 CA ARG 3 335,611 1 1,211 372,987 0.20 QQQ QQ C

ATOM 47 HA ARG 3 335.199 12.076 373.487 1.00 999.99 H

ATOM 48 CB ARG 3 337,142 11,195 373.104 0.20 QQQ OD C

ATOM 49 HB3 ARG 3 337.412 11.048 374.172 1.00 999.99 H

ATOM 50 HB2 ARG 3 337.553 10.346 372.515 1.00 999.99 H

ATOM 51 CG ARG 3 337,765 12,507 372,636 1.00 999.99 C ATOM 52 HG3 ARG 3 337.297 13.336 373.210 1.00 999.99 H

ATOM 53 HG2 ARG 3 337.545 12.664 371.560 1.00 999.99 H

ATOM 54 CD ARG 3 339.276 12.562 372.855 1.00 999.99 C

ATOM 55 HD3 ARG 3 339,523 12,421 373,929 1.00 QQQ QQ H

ATOM 56 HD2 ARG 3 339.807 11.809 372.234 1.00 999.99 H

ATOM 57 NE ARG 3 339.744 13.917 372.445 1.00 999.99 N

ATOM 58 HE ARG 3 339.086 14.584 372.096 1.00 999.99 H

ATOM 59 CZ ARG 3 341.064 14.251 372.562 1.00 999.99 C

ATOM 60 NH1 ARG 3 341.958 13.338 373.038 1.00 999.99 N

ATOM 61 HH11 ARG 3 340.826 16.172 371.871 1.00 999.99 H

ATOM 62 HH12 ARG 3 342.453 15.740 372.280 1.00 999.99 H

ATOM 63 NH2 ARG 3 341.485 15.498 372.204 1.00 999.99 N

ATOM 64 HH21 ARG 3 342.924 13.582 373.129 1.00 999.99 H

ATOM 65 HH22 ARG 3 341.647 12.423 373.297 1.00 999.99 H

ATOM 66 C ARG 3 335.249 11.250 371.544 0.20 999.99 C

ATOM 67 O ARG 3 335.080 12.313 370.949 0.20 999.99 O

ATOM 68 N TYR 4 335.115 10.051 370.954 0.20 102.96 N

ATOM 69 H TYR 4 335.245 9.201 371.459 1.00 102.96 H

ATOM 70 CA TYR 4 334.794 9.910 369.568 0.20 102.96 C

ATOM 71 HA TYR 4 335.560 10.407 368.991 1.00 102.96 H

ATOM 72 CB TYR 4 334.672 8.428 369.178 0.20 102.96 C

ATOM 73 HB3 TYR 4 335.637 7.897 369.319 1.00 102.96 H

ATOM 74 HB2 TYR 4 333.882 7.929 369.779 1.00 102.96 H

ATOM 75 CG TYR 4 334.289 8.321 367.747 0.20 102.96 C

ATOM 76 CD1 TYR 4 335.236 8.417 366.755 0.20 102.96 C

ATOM 77 HD1 TYR 4 336.271 8.581 367.015 1.00 102.96 H

ATOM 78 CD2 TYR 4 332.973 8.117 367.401 0.20 102.96 C

ATOM 79 HD2 TYR 4 332.226 8.041 368.177 1.00 102.96 H

ATOM 80 CE1 TYR 4 334.870 8.312 365.435 0.20 102.96 C

ATOM 81 HE1 TYR 4 335.622 8.388 364.664 1.00 102.96 H

ATOM 82 CE2 TYR 4 332.602 8.011 366.082 0.20 102.96 C

ATOM 83 HE2 TYR 4 331.565 7.849 365.827 1.00 102.96 H

ATOM 84 CZ TYR 4 333.556 8.105 365.096 0.20 102.96 C

ATOM 85 OH TYR 4 333.194 7.997 363.738 0.20 102.96 0

ATOM 86 HH TYR 4 334,000 8,027 363,216 1.00 102.96 H

ATOM 87 C TYR 4 333.472 10.564 369.324 0.20 102.96 C

ATOM 88 0 TYR 4 333.285 11.247 368.320 0.20 102.96 O

ATOM 89 N LYS 5 332.517 10.365 370.245 0.20 82.96 N

ATOM 90 H LYS 5 332.678 9.844 371.079 1.00 82.96 H

ATOM 91 CA LYS 5 331.205 10.923 370.105 0.20 82.96 C

ATOM 92 HA LYS 5 330.793 10.603 369.159 1.00 82.96 H

ATOM 93 CB LYS 5 330.286 10.548 371.279 0.20 82.96 C

ATOM 94 HB3 LYS 5 330.838 10.748 372.222 1.00 82.96 H

ATOM 95 HB2 LYS 5 329.390 11.202 371.263 1.00 82.96 H

ATOM 96 CG LYS 5 329.819 9.092 371.282 0.20 82.96 C ATOM 97 HG3 LYS 5 330.675 8.420 371.052 1.00 82.96 H

ATOM 98 HG2 LYS 5 329.052 8.965 370.487 1.00 82.96 H

ATOM 99 CD LYS 5 329.233 8.694 372.639 0.20 82.96 C

ATOM 100 HD3 LYS 5 330.058 8.714 373.384 1.00 82.96 H

ATOM 101 HD2 LYS 5 328.477 9.449 372.948 1.00 82.96

ATOM 102 CE LYS 5 328.581 7.308 372.660 0.20 82.96 C

ATOM 103 HE3 LYS 5 329.287 6.532 372.298 1.00 82.96 H

ATOM 104 HE2 LYS 5 328.247 7.051 373.688 1.00 82.96 H

ATOM 105 NZ LYS 5 327.386 7.287 371.785 0.20 82.96 N

ATOM 106 HZ1 LYS 5 326.968 6.335 371.789 1.00 82.96 H

ATOM 107 HZ2 LYS 5 327.659 7.539 370.813 1.00 82.96 H

ATOM 108 HZ3 LYS 5 326.686 7.972 372.136 1.00 82.96 H

ATOM 109 C LYS 5 331.289 12.414 370.118 0.20 82.96 C

ATOM 110 O LYS 5 330.610 13.075 369.335 0.20 82.96 O

ATOM 111 N ARG 6 332.130 12.982 371.007 0.20 91.69 N

ATOM 112 H ARG 6 332.721 12.454 371.610 1.00 91.69 H

ATOM 113 CA ARG 6 332.121 14.407 371.176 0.20 91.69 C

ATOM 114 HA ARG 6 331.141 14.696 371.527 1.00 91.69 H

ATOM 115 CB ARG 6 333.218 14.896 372.136 0.20 91.69 C

ATOM 116 HB3 ARG 6 334.208 14.595 371.729 1.00 91.69 H

ATOM 117 HB2 ARG 8 333.192 16.006 372.180 1.00 91.69 H

ATOM 118 CG ARG 6 333.105 14.356 373.562 0.20 91.69 C

ATOM 119 HG3 ARG 6 333.991 14.706 374.133 1.00 91.69 H

ATOM 120 HG2 ARG 6 333.124 13.244 373.541 1.00 91.69 H

ATOM 121 CD ARG 6 331.850 14.823 374.299 0.20 91.69 C

ATOM 122 HD3 ARG 6 331.778 15.932 374.305 1.00 91.69 H

ATOM 123 HD2 ARG 6 330.928 14.386 373.858 1.00 91.69 H

ATOM 124 NE ARG 6 331.961 14.361 375.713 0.20 91.69 N

ATOM 125 HE ARG 6 332.323 14.981 376.410 1.00 91.69 H

ATOM 126 CZ ARG 6 331.581 13.099 376.058 0.20 91.69 C

ATOM 127 NH1 ARG 6 331.093 12.244 375.112 0.20 91.69 N

ATOM 128 HH11 ARG 6 330.830 11.315 ^• 375.367 1.00 91.69 H

ATOM 129 HH12 ARG 6 331.004 12.546 374.162 1.00 91.69 H

ATOM 130 NH2 ARG 6 331.699 12.693 377.354 0.20 91.69 N

ATOM 131 HH21 ARG 6 332.065 13.321 378.041 1.00 91.69 H

ATOM 132 HH22 ARG 6 331.420 11.770 377.619 1.00 91.69 H

ATOM 133 C ARG 6 332 399 15.078 369.872 0.20 91.69 C

ATOM 134 0 ARG 6 331.567 15.827 369.364 0.20 91.69 O

ATOM 135 N ARG 7 333.574 14.815 369.281 0.20 272.70 N

ATOM 136 H ARG 7 334.255 14.196 369.666 1.00 272.70 H

ATOM 137 CA ARG 7 333.886 15.423 368.025 0.20 272.70 C

ATOM 138 HA ARG 7 334.541 14.573 367.905 1.00 272.70 H

ATOM 139 CB ARG 7 335.256 16.084 367.760 0.20 272.70 C

ATOM 140 HB3 ARG 7 335.614 16.579 368.688 1.00 272.70 H

ATOM 141 HB2 ARG 7 335.973 15.277 367.497 1.00 272.70 H ATOM 142 CG ARG 7 335.265 17.115 366.624 0.20 272.70 c

ATOM 143 HG3 ARG 7 336.329 17.321 366.381 1.00 272.70 H

ATOM 144 HG2 ARG 7 334.776 16.689 365.721 1.00 272.70 H

ATOM 145 CD ARG 7 334.638 18.470 366.976 0.20 272.70 C

ATOM 146 HD3 ARG 7 335.088 18.887 367.901 1.00 272.70 H

ATOM 147 HD2 ARG 7 334.773 19.190 366.141 1.00 272.70 H

ATOM 148 NE ARG 7 333.174 18.322 367.209 0.20 272.70 N

ATOM 149 HE ARG 7 332.713 17.460 367.003 1.00 272.70 H

ATOM 150 CZ ARG 7 332.468 19 392 367.683 0.20 272.70 C

ATOM 151 NH1 ARG 7 333.108 20.558 367.986 0.20 272.70 N

ATOM 152 HH11 ARG 7 332.587 21.341 368.328 1.00 272.70 H

ATOM 153 HH12 ARG 7 334.098 20.631 367.872 1.00 272.70 H

ATOM 154 NH2 ARG 7 331.117 19.299 367.854 0.20 272.70 N

ATOM 155 HH21 ARG 7 330.602 20.087 368.192 1.00 272.70 H

ATOM 156 HH22 ARG 7 330.642 18.450 367.628 1.00 272.70 H

ATOM 157 C ARG 7 333.109 14.928 366.860 0.20 272.70 C

ATOM 158 O ARG 7 332.702 15.685 365.979 0.20 272.70 O

ATOM 159 N LEU 8 332.877 13.605 366.858 0.20 101.17 N

ATOM 160 H LEU 8 333.188 13.024 367.804 1.00 101.17 H

ATOM 161 CA LEU 8 332.225 12.944 365.772 0.20 101.17 C

ATOM 162 HA LEU 8 332.296 11.881 365.950 1.00 101.17 H

ATOM 163 CB LEU 8 330.759 13.354 365.549 0.20 101.17 C

ATOM 164 HB3 LEU 8 330.169 13.168 366.475 1.00 101.17 H

ATOM 165 HB2 LEU 8 330.716 14.440 365.320 1.00 101.17 H

ATOM 166 CG LEU 8 330.141 12.560 364.384 0.20 101.17 C

ATOM 167 HG LEU 8 330.778 12.715 363.488 1.00 101.17 H

ATOM 168 CD1 LEU 8 330.138 11.062 364.716 0.20 101.17 C

ATOM 169 HD11 LEU 8 329.503 10.864 365.606 1.00 101.17 H

ATOM 170 HD12 LEU 8 331.170 10.714 364.935 1.00 101.17 H

ATOM 171 HD13 LEU 8 329.742 10.475 363.860 1.00 101.17 H

ATOM 172 CD2 LEU 8 328.728 13.061 364.047 0.20 101.17 C

ATOM 173 HD21 LEU 8 328.049 12.930 364.915 1.00 101.17 H

ATOM 174 HD22 LEU 8 328.321 12.488 363.188 1.00 101.17 H

ATOM 175 HD23 LEU 8 328.752 14.137 363.775 1.00 101.17 H

ATOM 176 C LEU 8 333.014 13.303 364.520 0.20 101.17 C

ATOM 177 0 LEU 8 332.412 13.866 363.567 0.20 101.17 0

ATOM 178 OXT LEU 8 334.242 13.022 364.505 1.00 101.17 0

END

An interaction may preferably be such that the interaction-inhibiting compound interacts with the ETR1 or its isoforms ERS1, ETR2, ERS2, EIN4 or a homologous or orthologous protein thereof. Most preferably, the interaction inhibiting compound binds to ETR1 or one of its isoforms ERS1, ETR2, ERS2, EIN4, or a homologous or orthogenic protein thereof. In particular, this prevents the interaction with the retarded signal component EIN2 or an orthologous protein thereof. Methods for determining whether a compound interacts with ETR1 or its isoforms ERS1, ETR2, ERS2, EIN4, or a homologous or orthologous protein thereof, are known to those skilled in the art. In particular, this is the isothermal

Titration calorimetry, as described, for example, in J.B. Chaires, Calorimetry and thermodynamics in drug design, Ann. Rev. Biophys., 37, 125-151 (2008). Further preferred methods are described in M.A. Coopler, Label-free Screening of Biomolecular Interactions, Anal. Bioanal. Chem., 337, 834-842 (2003) and M. Jerabek-Willemsen et al., Molecular interaction studies using microscale

thermosphoresis, ASSAY and drug development technologies, 9 (201 1) 342-353. Another preferred method is the thermophoresis. In a further preferred embodiment, the interaction inhibiting compound has a water solubility at pH = 7 and 20 ° C of at least 1 g / L, more preferably at least 10 g / L, most preferably at least 50 g / L on. In the known methods of the prior art, the competitive inhibition of the receptors by ethylene antagonists attached to the

Bind ethylene-binding site in the membrane domain of the receptors, the antagonists used must have hydrophobic properties. As a result, the known ethylene antagonists are usually poorly soluble in water, which is particularly the formulation of solutions for the treatment of plants and / or their

Fruit difficult (example: water solubility of 1 -MCP: 137mg / L at pH = 7 and 20 ° C). It has surprisingly been found that at

inventive method, the use of compounds having a

Water solubility of at least 1 g / L is advantageous. As a result, in particular the formulation of the treatment solution is much easier, since formulation based on water can be realized.

In a particularly preferred embodiment, the interaction inhibiting compound is selected from the group consisting of a peptide

Peptidomimetic, an antibody and / or its fragments and mixtures of these compounds. Very particularly preferred is the interaction inhibiting A compound selected from the group consisting of a peptide, a

 Peptidomimetic and mixtures of these compounds.

It is further preferred that the peptide, the antibody and / or its fragments are an isolated partial sequence of the protein EIN2 or an orthologous

Or a permutation of this partial sequence, or in that the peptide mimetic comprises a peptide backbone-modified, isolated partial sequence of the protein EIN2 or an orthologous protein thereof or a permutation of this partial sequence or a permutation thereof.

In this context, the term "isolated" in the sense of this invention means in particular that the subsequence of the EIN2 or the orthologous protein thereof naturally occurs in this protein but is provided in a modified form from this natural environment The subsequence is particularly free of other proteins, particularly preferably the isolated partial sequence or permutation thereof modified on the peptide backbone thereof in a highly pure form of greater than 95% purity, more preferably higher provided as 99% purity.

A "permutation" of the amino acid sequence in the context of the invention means a permutation which is only pronounced to the extent that the resulting amino acid sequence has the same biological activity as the original sequence an orthologous protein thereof, or the sequences SEQ ID NOS: 1 to 4, which are referred to later, is preferred as the sequence of origin of one of the sequences of SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 110, SEQ ID NO : 111, SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO: 114, SEQ ID NO: 115, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 118, SEQ ID NO: 119 , SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 or SEQ ID NO: 124. Preferably, a permutation of a sequence means that half, more preferably 2/3, entirely more preferably 3/4 and most preferably 90% of the amino acids over the Source sequence are not reversed. In a particularly preferred embodiment, the peptide, the antibody and / or its fragments comprises an isolated partial sequence or a permutation thereof which corresponds to the domain of EIN2 which interacts with the receptor protein ETR1 or the peptide mimetic comprises a peptide backbone modified, isolated partial sequence or a Permutation thereof, which corresponds to the domain of the EIN2 which interacts with the receptor protein ETR1.

Further preferably, the peptide, the antibody and / or its fragments comprises at least one amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3 or that

Peptide mimetic comprises at least one amino acid modified on the peptide backbone, which is selected from the group consisting of

Amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 8 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of

 Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3. In this case, compounds are excluded in which the peptide or antibody and / or its fragment has an amino acid sequence of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100 , SEQ ID NO: 101 or SEQ ID NO: 102, and / or a part of one of the

Amino acid sequences SEQ ID NO: 98 to SEQ ID NO: 102, which comprises at least 6 of the amino acids mentioned in SEQ ID NO: 98 to SEQ ID NO: 102 and / or comprises a derivative of the amino acid sequences SEQ ID NO: 98 to 102. Likewise, compounds are excluded in which the peptide mimetic from an am

Peptide backbone modified amino acid sequence consists of which is selected of the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 102. Particular preference is also given to compounds in which the peptide mimetic comprises one on the peptide backbone modified amino acid sequence which is selected from a part of one of the amino acid sequences SEQ ID NO: 98 to SEQ ID NO: 102, which comprises at least 6 of the amino acids mentioned in SEQ ID NO: 98 to SEQ ID NO: 102. Particular preference is also given to compounds in which the peptide mimetic consists of an amino acid sequence modified on the peptide backbone which is selected from a derivative of the amino acid sequences SEQ ID NO: 98 to 102.

Also preferably, the peptide, the antibody and / or its fragments comprises at least one amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 103, a part of

Amino acid sequence SEQ ID NO: 103, which comprises at least 4, preferably at least 5, particularly preferably at least 6, of the amino acids mentioned in SEQ ID NO: 103, and a derivative of the amino acid sequence SEQ ID NO: 103, where if the amino acid sequence SEQ ID NO: 103 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 103 is alanine.

Furthermore, the peptide, the antibody and / or its fragments preferably comprise at least one amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 103, a part of

Amino acid sequence SEQ ID NO: 103, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 103, and a derivative of the amino acid sequence SEQ ID NO: 103, provided that when the amino acid sequence SEQ ID NO: 103 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 103 is alanine, and provided that the positions identified by SEQ ID NO: 03 with No. 6 and No. 7 are present these are either either arginine or both histidine.

For the purposes of the present invention, the "position" of an amino acid means the site which is under counting when reading the sequence from left to right of the amino acids. Thus, for example, an octapeptide from left to right comprises positions 1 to 8. If in the context of the present invention alanine is mentioned at one position, this means that in the given SEQ ID, according to its definition, at least one amino acid can be alanine. However, if the sequence contains alanine at one site, it will not contain alanine as the amino acid at any other of the possible amino acids according to SEQ ID. This means that of the defined choices, the amino acid alanine can preferably be selected only once. Also preferably, the peptide, the antibody and / or its fragments comprises at least one amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 104, a part of

Amino acid sequence SEQ ID NO: 104, which comprises at least 4, preferably at least 5, particularly preferably at least 6, of the amino acids mentioned in SEQ ID NO: 104, and a derivative of the amirous acid sequence SEQ ID NO: 104, where, when the amino acid sequence SEQ ID NO: 104 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 104 is alanine

Furthermore, preferably, the peptide, the antibody and / or its fragments comprises at least one amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 104, a part of

Amino acid sequence SEQ ID NO: 104, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 104, and a derivative of the amino acid sequence SEQ ID NO: 104, provided that when the amino acid sequence SEQ ID NO: 104 at a

Alanine, none of the other amino acids of SEQ ID NO: 104 being alanine, and provided that when the positions indicated by SEQ ID NO: 104 are Nos. 6 and 7, they are either either arginine or both are histidine.

Also preferably, the peptide, the antibody and / or its fragments comprises at least one amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 105, a part of

Amino acid sequence SEQ ID NO: 105, which is at least 4, preferably at least 5, particularly preferably at least 6 of the amino acids mentioned in SEQ ID NO: 105 comprises »and a derivative of the amino acid sequence SEQ ID NO: 105, wherein _» if the amino acid sequence SEQ ID NO: 105 comprises alanine at one position, none of the other amino acids of SEQ ID NO : 105 Alanin is.

Also preferably, the peptide, the antibody and / or its fragments comprises at least one amino acid sequence _"is that selected from the group consisting of the amino acid sequence SEQ ID NO: 106, a portion of the

Amiriosäuresequenz SEQ ID NO: 106, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 108 _» and a derivative of the amino acid sequence SEQ ID NO: 106 _» wherein when the amino acid sequence SEQ ID NO: 108 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 106 is alanine. Also preferably, the peptide, the antibody and / or its fragments comprises at least one amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 107, a part of

Amino acid sequence SEQ ID NO: 107, which comprises at least 4, preferably at least 5, particularly preferably at least 8, of the amino acids mentioned in SEQ ID NO: 107, and a derivative of the amino acid sequence SEQ ID NO: 1087, where if the amino acid sequence SEQ ID NO: 107 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 107 is alanine.

Also preferably, the peptide, the antibody and / or its fragments comprises at least one amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 108 _» a part of

Amino acid sequence SEQ ID NO: 108, comprising at least 4 _" preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 108, and a derivative of the amino acid sequence SEQ ID NO: 108, wherein when the amino acid sequence SEQ ID NO: 108 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 108 is alanine.

Most preferably, the peptide, the antibody and / or its fragments comprise at least one amino acid sequence selected from the group consisting of consisting of SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 1 10, SEQ ID NO: 11 1, SEQ ID NO: 1 12, SEQ ID NO: 1 13, SEQ ID NO: 1 14, SEQ ID NO: 1 15, SEQ ID NO: 1 16, SEQ ID NO: 1 17, SEQ ID NO: 1 18, SEQ ID NO: 1 19, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, a permutation of one of the amino acid sequences SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 1 10, SEQ ID NO: 1 1 1, SEQ ID NO: 1 12, SEQ ID NO: 1 13, SEQ ID NO: 1 14, SEQ ID NO: 1 15, SEQ ID NO: 1 16, SEQ ID NO: 1 17, SEQ ID NO: 1 18, SEQ ID NO: 1 19, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, a part of one of the amino acid sequences SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 1 10, SEQ ID NO: 1 1 1, SEQ ID NO: 1 12, SEQ ID NO: 1 13, SEQ ID NO: 1 14, SEQ ID NO: 1 15, SEQ ID NO: 1 16, SEQ ID NO: 1 17, SEQ ID NO: 1 18, SEQ ID NO: 1 19, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, which at least 4, preferably mindes at least 5, particularly preferably at least 6, of the amino acids mentioned in SEQ ID NO: 4, SEQ ID NO: 109 to SEQ ID NO: 124, and a derivative of one of the amino acid sequences SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 1 10, SEQ ID NO: 1 11, SEQ ID NO: 1 12, SEQ ID NO: 1 13, SEQ ID NO: 1 14, SEQ ID NO: 1 15, SEQ ID NO: 1 16, SEQ ID NO 1 17, SEQ ID NO: 1 18, SEQ ID NO: 1 19, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124.

Likewise preferably, the aptamer is prepared on the basis of the target structure of a peptide, wherein the peptide is selected from the amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amirous acid sequence SEQ ID NO: 3, a permutation of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which at least 4, preferably at least 5, particularly preferably at least 6 in SEQ ID NO: 1 to SEQ ID NO 3 amino acids, and a derivative of one of the amino acid sequences of SEQ ID NO: 1 to SEQ ID NO: 3. Excluded are compounds in which an aptamer is prepared on the basis of the target structure of a peptide, wherein the peptide is selected from the A group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100 SEQ ID NO: 101 and SEQ ID NO: 102. Also preferred are compounds in which an aptamer is prepared based on the target structure of a peptide The peptide is selected from a part of one of the amino acid sequences SEQ ID NO: 98 to SEQ ID NO: 102, which at least 6 of the amino acids mentioned in SEQ ID NO: 98 to SEQ ID NO: 102, consists. Preference is also given to compounds in which an aptamer based on the target structure of a peptide is prepared, the peptide consisting of a derivative of the amino acid sequences SEQ ID NO: 98 to 102.

Also preferably, the aptamer is prepared based on the target structure of a peptide, wherein the peptide is selected from the group consisting of the amino acid sequence SEQ ID NO: 103, a portion of the amino acid sequence SEQ ID NO: 103, which at least 4, preferably at least 5 , particularly preferably at least 6 of the amino acids mentioned in SEQ ID NO: 103, and a derivative of the amino acid sequence SEQ ID NO: 103, wherein, when the

Amino acid sequence SEQ ID NO: 103 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 103 is alanine. Also preferred is the aptamer based on the target structure of a peptide

wherein the peptide is selected from the group consisting of the amino acid sequence SEQ ID NO: 103, a part of the amino acid sequence SEQ ID NO: 103, which at least 4, preferably at least 5, more preferably at least 6 of the in SEQ ID NO: 103 amino acid sequence, and a derivative of the amino acid sequence SEQ ID NO: 103, provided that when the amino acid sequence SEQ ID NO: 103 comprises alanine at one position, none of the other amino acids of SEQ ID NO: 103 is alanine and of the

Provided that when in SEQ ID NO: 103 with No. 6 and No. 7

characterized positions are present, these are either both arginine or both histidine.

Also preferred is the aptamer based on the target structure of a peptide

wherein the peptide is selected from the group consisting of the amino acid sequence SEQ ID NO: 104, a part of the amino acid sequence SEQ ID NO: 104, which at least 4, preferably at least 5, particularly preferably at least 6 of the in SEQ ID NO: 104 amino acid sequence, and a derivative of the amino acid sequence SEQ ID NO: 104, wherein, when the

Amino acid sequence SEQ ID NO: 104 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 104 is alanine. Also preferably, the aptamer is prepared based on the target structure of a peptide, wherein the peptide is selected from the group consisting of the amino acid sequence SEQ ID NO: 104, a portion of the amino acid sequence SEQ ID NO: 104, which at least 4, preferably at least 5 , more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 104, and a derivative of the amino acid sequence SEQ ID NO: 104, provided that when the amino acid sequence SEQ ID NO: 104 at one position comprises alanine, none of the others Amino acids of SEQ ID NO: 104 is alanine, and provided that when the positions identified in SEQ ID NO: 104 with No. 6 and No. 7 are present, they are either both arginine or both histidine.

Also preferably, the aptamer is prepared based on the target structure of a peptide, wherein the peptide is selected from the group consisting of the amino acid sequence SEQ ID NO: 105, a portion of the amino acid sequence SEQ ID NO: 105, which at least 4, preferably at least 5 , particularly preferably at least 6 of the amino acids mentioned in SEQ ID NO: 105, and a derivative of the amino acid sequence SEQ ID NO: 105, wherein, when the

Amino acid sequence SEQ ID NO: 105 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 105 is alanine.

Also preferably, the aptamer is prepared based on the target structure of a peptide, wherein the peptide is selected from the group consisting of the amino acid sequence SEQ ID NO: 106, a portion of the amino acid sequence SEQ ID NO: 106, which at least 4, preferably at least 5 , particularly preferably at least 6 of the amino acids mentioned in SEQ ID NO: 106, and a derivative of the amino acid sequence SEQ ID NO: 106, wherein, when the

Amino acid sequence SEQ ID NO: 106 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 106 is alanine.

Also preferably, the aptamer is prepared based on the target structure of a peptide, wherein the peptide is selected from the group consisting of the amino acid sequence SEQ ID NO: 107, a portion of the amino acid sequence SEQ ID NO: 107, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 107, and a derivative of the amino acid sequence SEQ ID NO: 107, wherein, when the

Amino acid sequence SEQ ID NO: 107 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 107 is alanine.

Also preferably, the aptamer is prepared based on the target structure of a peptide, wherein the peptide is selected from the group consisting of the amino acid sequence SEQ ID NO: 108, a portion of the amino acid sequence SEQ ID NO: 108, which at least 4, preferably at least 5 , more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 108, and a derivative of the amino acid sequence SEQ ID NO: 108, wherein, when the

Amino acid sequence SEQ ID NO: 108 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 108 is alanine.

Most preferably, the aptamer becomes based on the target structure of a peptide

prepared, wherein the peptide is selected from the group consisting of SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 1 10, SEQ ID NO: 11, SEQ ID NO: 1 12, SEQ ID NO SEQ ID NO: 1,13, SEQ ID NO: 1,17, SEQ ID NO: 1,17, SEQ ID NO: 1,18, SEQ ID NO: 1,19, SEQ ID NO: 1. 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, a permutation of one of

Amino acid sequences SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 1 10, SEQ ID NO: 1 1 1, SEQ ID NO: 1 12, SEQ ID NO: 1 13, SEQ ID NO: 1 14, SEQ ID NO: 1 15, SEQ ID NO: 1 16, SEQ ID NO: 1 17, SEQ ID NO: 1 18, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122 , SEQ ID NO: 123 and SEQ ID NO: 124, a part of one of the amino acid sequences SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 1 10, SEQ ID NO: 1 1 1, SEQ ID NO: 112 , SEQ ID NO: 1 13, SEQ ID NO: 1 14, SEQ ID NO: 1 15, SEQ ID NO: 1 16, SEQ ID NO: 1217, SEQ ID NO: 1 18, SEQ ID NO: 1 19, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, which at least 4, preferably at least 5, particularly preferably at least 6 of in SEQ ID NO: 4, SEQ ID NO: 109 to SEQ ID NO: 124, and a derivative of one of the amino acid sequences SEQ ID NO: 4, 1 SEQ ID NO: 109, SEQ ID NO: 1 10, SEQ ID NO: 1 1 1, SEQ ID NO: 1 12, SEQ ID NO: 1 13, SEQ ID NO: 1 14, SEQ ID NO: 1 15, SEQ ID NO: 1 16, SEQ ID NO: 1 17, SEQ ID NO: 1 18, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124.

The aptamer is very particularly preferably produced on the basis of the target structure of a peptide, wherein the peptide is selected _'from the group consisting of SEQ ID NO: 4, a permutation of the amino acid sequence SEQ ID NO: 4, a portion of the amino acid sequence SEQ ID NO: 4, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 4, and a derivative of the amino acid sequence SEQ ID NO: 4.

It is particularly preferred that the peptide, the antibody and / or its fragments in addition to the at least one amino acid sequence mentioned at least 4 further, preferably at least 3 further, most preferably at least 2 further natural amino acids. Preferably, the term "comprising" means that the sequence of 4 further amino acids, preferably at least 3 further, most preferably at least 2 further, most preferably 2 further natural amino acids to those in the corresponding

Amino acid sequence indicated. A derivative of an amino acid sequence is preferably considered to be a compound which has an organic group which is different from an amino acid on at least one terminus, ie its C- and / or N-terminus of the sequence. This organic group may preferably be RY- wherein R is a hydrophobic residue and Y is a spacer attached to the C and / or N-terminus. It is particularly preferred that the resulting derivative of the

 Amino acid sequence has a solubility of at least 1 g / L at 20 ° C and pH = 7. Y is preferably selected from the group consisting of -O-, -C (= O) - or -C (= O) -NH-. R is preferably an aliphatic or aromatic, linear, branched or cyclic hydrocarbon radical which may optionally have alkenyl or alkynyl groups. Particularly preferably, the

Hydrocarbon radical 2 to 12 carbon atoms. The group RY, depending on where it is present, at the C-terminus is the same as or different from the group RY at the N-terminus. In one embodiment, the peptide mimetic is particularly a peptoid or D-peptide having a similar biological activity to an amino acid sequence selected from the group consisting of

Amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of

 Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 8 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3. Excluded are compounds in which the peptide mimetic consists of a peptide backbone

modified amino acid sequence which is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 102. Preference is also given to compounds except in in which the peptide mimetic consists of an amino acid sequence modified on the peptide backbone, which is selected from a part of one of the amino acid sequences SEQ ID NO: 98 to SEQ ID NO: 102, which comprises at least 6 of the amino acids mentioned in SEQ ID NO: 98 to SEQ ID NO: 102 includes. Preference is also given to compounds in which the peptide mimetic consists of an amino acid sequence modified on the peptide backbone, which is selected from a derivative of the amirous acid sequences SEQ ID NO: 98 to 102.

In another embodiment, the peptide mimetic is in particular a peptoid or D-peptide which has a similar biological activity as a

Amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 103, a part of the amino acid sequence SEQ ID NO: 103, which at least 4, preferably at least 5, more preferably at least 8 of the mentioned in SEQ ID NO: 103 Amino acid, and a derivative of the amino acid sequence of SEQ ID NO: 103, wherein, when the

Amino acid sequence SEQ ID NO: 103 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 103 is aianin.

The peptide mimetic preferably represents in particular a peptoid or D-peptide which have a similar biological activity to an amino acid sequence, which is selected from the group consisting of the amino acid sequence SEQ ID NO: 103, a part of the amino acid sequence SEQ ID NO: 103 which comprises at least 4, preferably at least 5, more preferably at least 8 of the amino acids mentioned in SEQ ID NO: 103, and a derivative of the amirous acid sequence SEQ ID NO: 103, with the proviso that when the amino acid sequence SEQ ID NO: 103 at one position comprises alanine, ^' none of the other amino acids of SEQ ID NO: 103 is alanine and provided that when the positions indicated by SEQ ID NO: 103 are Nos. 6 and Nos. 7, these are either either arginine or both histidine.

Also preferably, the peptide mimetic is, in particular, a peptoid or D-peptide which has a similar biological activity to an amino acid sequence

which is selected from the group consisting of

Amino acid sequence SEQ ID NO: 104, a part of the amino acid sequence SEQ ID NO: 104, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 104, and a derivative of the amino acid sequence SEQ ID NO: 101 , where if the

Amino acid sequence SEQ ID NO: 101 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 101 is alanine.

Also preferably, the peptide mimetic is, in particular, a peptoid or D-peptide which has a similar biological activity to an amino acid sequence

which is selected from the group consisting of

Amino acid sequence SEQ ID NO: 104, a part of the amino acid sequence SEQ ID NO: 104, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 104, and a derivative of the amino acid sequence SEQ ID NO: 104 with the proviso that when the amino acid sequence of SEQ ID NO: 104 comprises alanine at one position, none of the other amino acids of SEQ ID NO: 104 is alanine and under the

Provided that, if in SEQ ID NO: 104 with No. 6 and No. 7

characterized positions are present, these are either both arginine or both histidine. Also preferably, the peptide mimetic is in particular a peptoid or D-peptide having a similar biological activity to an amino acid sequence selected from the group consisting of

Amino acid sequence SEQ ID NO: 105, a part of the amino acid sequence SEQ ID NO: 105 which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 105, and a derivative of the amirous acid sequence SEQ ID NO: 05 , where if the

Amino acid sequence SEQ ID NO: 05 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 105 is alanine.

Also preferably, the peptide mimetic represents in particular a peptoid or D-peptide having a similar biological activity as an amino acid sequence selected from the group consisting of

Amino acid sequence SEQ ID NO. 106, a part of the amino acid sequence SEQ ID NO: 106, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 106, and a derivative of the amino acid sequence SEQ ID NO: 106, wherein if

Amino acid sequence SEQ ID NO: 106 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 106 is alanine.

Also preferably, the peptide mimetic represents in particular a peptoid or D-peptide having a similar biological activity as an amino acid sequence selected from the group consisting of

Amino acid sequence SEQ ID NO: 107, a part of the amino acid sequence SEQ ID NO: 107 which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 107, and a derivative of the amino acid sequence SEQ ID NO: 107 , where if the

Amino acid sequence SEQ ID NO: 107 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 107 is alanine.

Also preferably, the peptide mimetic is in particular a peptoid or D-peptide which has a similar biological activity to an amino acid sequence

which is selected from the group consisting of

Amino acid sequence SEQ ID NO: 108, a part of the amino acid sequence SEQ ID NO: 108, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 108, and a derivative of the amirous acid sequence SEQ ID NO: 108, wherein, if the

Amino acid sequence SEQ ID NO: 108 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 108 is alanine.

Most preferably, the peptide mimetic represents a peptoid or D-peptide having a similar biological activity to an amino acid sequence

which is selected from the group consisting of SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 110, SEQ ID NO: 11, SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO: 114, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 117, SEQ ID NO: 118, SEQ ID NO: 1 19, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, a permutation of one of the amino acid sequences SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 1 10, SEQ ID NO: 11, SEQ ID NO: 1 12, SEQ ID NO: 1 13, SEQ ID NO: 114, SEQ ID NO: 1 15, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 1 18, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, a part of one of

Amino acid sequences SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 110, SEQ ID NO: 111, SEQ ID NO: 112, SEQ ID NO: 1 13, SEQ ID NO: 1 14, SEQ ID NO: 115 , SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 1 18, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, which comprises at least 4, preferably at least 5, particularly preferably at least 6, of the amino acids mentioned in SEQ ID NO: 4, SEQ ID NO: 109 to SEQ ID NO: 124, and a derivative of one of the amino acid sequences SEQ ID NO : 4, SEQ ID NO: 109, SEQ ID NO: 110, SEQ ID NO: 111, SEQ ID NO: 112, SEQ ID NO: 13, SEQ ID NO: 114, SEQ ID NO: 115, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 118, SEQ ID NO: 1 19, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO : 124.

 The amirous acid sequence SEQ ID NO: 1 may also be represented as sequence xx [PLVIF] [KR] [RKW] x [RK] [RK] [RK] [PL] xx

In this case, each x is any natural amino acid. In addition to the proteinogenic amino acids, x preferably also contains natural, non-natural proteinogenic amino acids found in plants. Preferably, each x may be independently selected from the group consisting of alanine, arginine, asparagine, aspartic acid, cysteine, glutamine, glutamic acid, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, proline, serine, threonine, tryptophan, Tyrosine, valine, citrulline, ornithine, ε-acetyl-lysine, 3-aminopropionic acid (β-alanine), aminobenzoic acid, 6-aminocaproic acid, aminobutyric acid, hydroxyproline, mercaptopropionic acid, 3-nitro-tyrosine, norleucine and pyroglutamic acid. The square brackets of said sequence mean that the actual amino acid can be selected from the amino acids listed in the square brackets. Thus, the amino acids listed in square brackets are to be understood as having an "or" linked together

One-letter code for amino acids in which P is proline, L is leucine, V is valine, I is isoleucine, F is phenylalanine, K is lysine, R is arginine and W is tryptophan. The amino acid sequence SEQ ID NO: 1 does not include an amino acid sequence which is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 102 ,

Accordingly, the amino acid sequence SEQ ID NO: 2 can also be represented as x [PLVIF] [KR] [RKW] x [RK] [RK] [RK] [PL] x and the amino acid sequence SEQ ID NO: 3 also as

[PLVIF] [KR] [RKW] x [RK] [RK] [RK] [PL]

The amino acid sequences SEQ ID NO: 2 and / or 3 include none

An amino acid sequence selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 102. Most preferably, the peptide, the antibody and or its fragments at least one amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 3, a permutation of

Amino acid sequence SEQ ID NO: 3, a part of the amino acid sequence SEQ ID NO: 3, which at least 4, preferably at least 5, more preferably at least 6 the amino acid mentioned in SEQ ID NO: 3, and a derivative of the

Amino acid sequences SEQ ID NO: 3 or that the peptide mimetic comprises at least one peptide backbone modified amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 3, a permutation of the amino acid sequence SEQ ID NO: 3, a part of

 Amino acid sequence SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 3, and a derivative of the amino acid sequences SEQ ID NO: 3. In this case, the amino acid sequence SEQ ID NO: 3 no amirous acid sequence selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 102

Amino acid sequence SEQ ID NO: 3 also no part of a Amiriosäuresequenz comprising at least 6 of the mentioned in SEQ ID NO: 98 to 102 amino acids. Further preferably, the peptide, the antibody and / or its fragments also do not comprise a derivative of the amino acid sequence SEQ ID NO: 98 to 102. Also preferably, the aptamer is prepared on the basis of the target structure of a peptide, wherein the peptide is selected from the amino acid sequence SEQ ID NO: 3, a permutation of one of the amino acid sequence SEQ ID NO: 3, a part of one of the amino acid sequences SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 3, and a derivative of one of the amino acid sequence SEQ ID NO: 3

Amino acid sequences SEQ ID NO: 3 no amino acid sequence which is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 102 it prefers that

Amino acid sequence SEQ ID NO: 103 also does not comprise any part of an amino acid sequence which comprises at least 6 of the amino acids mentioned in SEQ ID NO: 98 to 102. Further preferably, the amino acid sequence SEQ ID NO: 3 also does not comprise a derivative of the amino acid sequence SEQ ID NO: 98 to 102. Most preferably, the peptide consists of an amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 3, a permutation of the amino acid sequence SEQ ID NO: 3, a part of the amino acid sequence SEQ ID NO: 3, which at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 3 and a derivative of the amino acid sequences of SEQ ID NO: 3 or that the peptide mimetic consists of a peptide backbone modified amino acid sequence selected from the group consisting of

Amino acid sequence SEQ ID NO: 3, a permutation of the amino acid sequence SEQ ID NO: 3, a part of the amino acid sequence SEQ ID NO: 3, which

at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 3, and a derivative of the

Amino acid sequences SEQ ID NO: 3. The amino acid sequence SEQ ID NO: 3 does not include an amino acid sequence which is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 102 and / or no part of an amino acid sequence which comprises at least 6 of the amino acids mentioned in SEQ ID NO: 98 to 102 and / or no derivative of the amino acid sequences SEQ ID NO: 98 to 102. In a very particular In a preferred embodiment, the interaction-inhibiting compound has the amino acid sequence SEQ ID NO: 4, a part of the amino acid sequence SEQ ID NO: 4 which comprises at least 4, preferably at least 5, particularly preferably at least 6 of the amino acids mentioned in SEQ ID NO: 4. Analogously to the statements above, the amino acid sequence SEQ ID NO: 4 can also be represented by the sequence

LKRYKRRL

Likewise, the amino acid sequences SEQ ID NO: 103 to 124 can be represented as follows:

 [LA] [KHRA] [RVHA] [KYA] [NKLFHA] [RHA] [RHA] [LA] SEQ ID NO: 103

[LA] [KA] [RVHA] [KYA] [NKLFHA] [RHA] [RHA] [LA] SEQ ID NO: 104

[LA] [KA] [RVHA] [KYA] [NKLFHA] [RA] [RA] [LA] SEQ ID NO: 105

[LA] [KA] [RVA] [KYA] [NKLFHA] [RA] [RA] [LA] SEQ ID NO: 106 [LA] [KA] [RA] [KA] [NKLFHA] [RA] [RA] [LA] SEQ ID NO: 107

[LA] [KA] [RA] [KA] [NKA] [RA] [RA] [LA] SEQ ID NO: 108

LKRKNRRL SEQ ID NO: 109

LKRKKRRL SEQ ID NO: 110

LKVYKRRL SEQ ID NO: 111 LKRKLRRL SEQ ID NO: 112

LKRKFRRL SEQ ID NO: 113

LHRYHRRL SEQ ID NO: 114

LRHYKHHL SEQ ID NO: 1145

KRYKRR SEQ ID NO: 116

AKRYKRRL SEQ ID NO: 127

LARYKRRL SEQ ID NO: 128

LKAYKRRL SEQ ID NO: 129

LKRAKRRL SEQ ID NO: 120

LKRYARRL SEQ ID NO: 121

LKRYKARL SEQ ID NO: 122

LKRYKRAL SEQ ID NO: 123

LKRYKRRA SEQ ID NO: 124 In another aspect of the present invention is a compound

which is selected from the group consisting of a peptide, a peptide mimetic and an aptamer, characterized in that the peptide consists of an amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 1, the

Amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, that the

Peptide mimetic consists of a peptide backbone modified amino acid sequence which is selected from the group consisting of

Amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3 or that the aptamer Based on the target structure of a peptide is prepared _" wherein the peptide is selected from the amino acid sequence SEQ ID NO: 1, the amino acid sequence

SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3. In this case, compounds are excluded in which the peptide from an amino acid sequence of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 or SEQ ID NO: 102, and / or from a part of one of the amino acid sequences SEQ ID NO: 98 to SEQ ID NO: 102, which comprises at least 6 of the amino acids mentioned in SEQ ID NO: 98 to SEQ ID NO: 102 and / or from a derivative of the amino acid sequences SEQ ID NO: 98 to 102 and / or in which a peptide mimetic consists of an am

Peptide backbone modified amino acid sequence which is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 102, and / or in which Aptamer is prepared based on the target structure of a peptide, wherein the peptide is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100 SEQ ID NO: 101 and SEQ ID NO: 102.

In this case, the compound is preferably isolated. Likewise, the connection is in the

Essentially cleaned. This means in particular that the compound is provided in a highly pure form of greater than 95% purity, more preferably greater than 99% purity.

Ethylene signal chain

The ethylene signal chain has been studied in the model plant Arabidopsis thaliana. Here, the membrane protein "Ethylene insensitive 2" (EIN2) could be identified as a central element of this chain (J.M. Alonso, T. Hiryama, G.

Roman, S. Nourizadeh, JR Ecker, EIN2, a bifunctional transducer of ethylene and stress responses in Arabidopsis, Science: 284, 2148-2152; 1999). So far, direct interactions between the different ethylene receptors and the protein IN2 following in the signal chain (M.Bisson, A. Bleckmann, S. Allekotte, G. Groth, EIN2, the central regulator of ethylene signaling, is localized at the ER membrane where it interacts with the ethylene receptor ETR1, Biochem J: 424, 1-6, 2009, and MMA Bisson, G. Groth, New insight in ethylene signaling: autokinase activity of ETR1 modulates the interaction of receptors and EIN2, Molecular Plant: 5,882-889, 2010). Ethylene resistant 1 (ETR1), Ethylene resistant 2 (ETR2), Ethylene response sensor (ERS1), Ethylene response sensor 2 (ERS2), and ethylene are known as ethylene receptors identified in Arabidopsis thaliana insensitive 4 "(EIN4) (MM Bisson, G. Groth, New paradigm in ethylene signaling, Plant Signal & Behav 6: 164-166; 2011). Nevertheless, the exact role of EIN2 and the underlying molecular mechanism of signal transduction are known still unknown at the ER membrane.

It could be shown that the method of the present invention leads to a disruption of the signal transduction important interaction of the receptor protein ETR1 or its isoforms ERS1, ETR2, ERS2, EIN4 or a homologous or orthologous protein thereof with the protein EIN2 or an orthologous protein thereof , By interrupting this signal path according to the invention, it has been possible to influence the maturation process, senescence process and / or the stress tolerance of plants and / or their fruits.

Homologous and orthologous proteins are characterized as having the same biological activity in a different species as a particular protein (e.g., ETR1) in a particular species (e.g., Arabidopsis).

For the purposes of this invention, a "homologous protein" is understood as meaning a protein with significant structural homology to the protein ETR1, in particular an identity of more than 70%, preferably more than 75%, more preferably more than 80% and most preferably more than 90%. with the protein ETR1

Understood. Methods for determining the homology of proteins are the

Specialist known. Frequently, homologous proteins are identified by a statistically significant number of amino acids. In particular, the BLAST (Basic Local Alignment Search Tool) algorithm can be used (S.F.

Altschul, W. Gish, W. Miller, EW Myers, DJ Lipman, Basic local alignment search tool. J, Mol. Biol. 215, 403-410; 1990). This identifies regions that have local similarities between sequences. The program compares the protein sequence with sequences in databases and calculates the statistical significance of the match.

Species having such identities are shown in Table 1 below (see also Figure 1). They are stored in known databases (YDR PDR protein database, UniProt or NCBi (National Center for Biotechnology Information)) under the specified entries:

Table 2: Homologous proteins of ETR1

Organism% identity to amino acid sequence deposit

 Arabidopsis number (Database Accession

ETR1 No.)

 Arabidopsis 100 SEQ ID NO: 5 UniProtKB / Swiss Prot thaliana P49333

 Malus x 83.33 SEQ ID NO: 6 GenBank: AAC31 123.1 domestica

 Brassica 96.46 SEQ ID NO: 7 UniProtKB / Swiss Prot: oleracea 049230.1

 Citrus hybrid 84.42 SEQ ID NO: 8 GenBank: ADB25217.1 cultivar

 Coffea 81.98 SEQ ID NO: 9 GenBank: ABL63471.1 canephora

 Cucumis sativus 82.25 SEQ ID NO: 10 UniProtKB / Swiss-Prot:

 Q9SSY6.1

 Dimocarpus 86.18 SEQ ID NO: 11 GenBank: ACL81480.3 longan

 Diospyros kaki 80.08 SEQ ID NO: 12 GenBank: BAE46932.1

Pelargonium x 81.03 SEQ ID NO: 13 UniProtKB / Swiss-Prot: hortum Q9XH58.1

 Hevea 81.71 SEQ ID NO: 14 GenBank: AAW31759.1 brasiliensis

Actin idia 84.15 SEQ ID NO: 15 GenBank: ABY28264.1 deliciosa Organism% identity to amino acid sequence deposit

 Arabidopsis number (Database Accession

ETR1 No.)

 Lactuca sativa 78.83 SEQ ID NO: 16 GenBank: AAQ15122.1

Mangifera indica 82.79 SEQ ID NO: 17 GenBank ;: AAF61919.1

Cucumis melo 82.79 SEQ ID NO: 18 GenBank: AAC99645.1 var.

cantalupensis

 Oryza sativa 72.17 SEQ ID NO: 19 GenBank: ABF98411.1

Passiflora edulis 62.60 SEQ ID NO: 20 UniProtKB / Swiss-Prot:

 Q9ZWL6.1

 Prunus persica 67.34 SEQ ID NO: 21 UniProtKB / Swiss-Prot:

 Q9M7M1.1

 Petunia x 81.28 SEQ ID NO: 22 GenBank: AAL40902.1 hybrida

 Prunus salicina 84.82 SEQ ID NO: 23 GenBank: ABU68266.1

Ricinus 40.51 SEQ ID NO: 24 NCBI Reference communis Sequence:

 XP_002529316.1

Glycine max 81.02 SEQ ID NO: 25 GenBank: ABR67685.1

Fragaria x 84.01 SEQ ID NO: 26 GenBank: CAC48384.1 |

Nicotiana 81.79 SEQ ID NO: 27 UniProtKB / Swiss-Prot: tabacum 048929.1

 Solanum 81.44 SEQ ID NO: 28 GenBank: AAC02213.1 iypersicum

 Vitis vinifera 83.06 SEQ ID NO: 29 NCBI Reference

 Sequence:

 XP_002277460.1

 Zea mays 37.80 SEQ ID NO: 30 GenBank: AAR25569.1

Particular preference is given to homologous proteins of the ETR1 selected from the group consisting of SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25 _» SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28,

SEQ ID NO: 29 and SEQ ID NO: 30. By "orthologous protein" is meant a protein that is the functional counterpart of another protein (ETR1 or EIN2) in another species. Sequence differences between the orthologs are the result of speciation. Methods for the identification of orthologous proteins are known in the art. Frequently, identification of orthologous proteins is based on the

BLAST (Basic Local Alignment Search Tool) algorithm. Further methods are described in Chen.F., Mackey, AJ _f Vermunt.JK, Roos.DS (2007) Assessing Performance of Orthologic Detection Strategies Applied to Eukaryotic Genomes, PLoS ONE, 2, e383; Tatusov.RL, Fedorova.ND, Jackson.JD, Jacobs.AR, Kiryutin.B., Koonin.EV, Krylov.DM, Mazumder.R., Mekhedov.SL, Nikolskaya.AN, et al. (2003) The COG database: an updated version includes eukaryotes. BMC Bioinformatics, 4, 41; Tatusov.RL, Koonin.EV and Lipman.DJ (1997) A genomic perspective on protein famiiies, Science, 278, 631; Altschul, SF, Madden.TL, Schaffer, AA,

Zhang J., Miller.W. and Lipman.D.J. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucleic Acids Res, 25, 3389;

Chen.F., Mackey.A.J., Stoeckert.C.J. Jr and Roos.D.S. (2006) OrthoMCL-DB: querying a comprehensive multi-species collection of orthologue groups. Nucleic Acids Res, 34, D363; Sonnhammer.E.L. and Koonin.E.V. (2002) Orthology, paralogy and proposed Classification for paralog subtypes. Trends Genet, 18, 619; O'Brien.K.P., Remm.M. and Sonnhammer.E.L. (2005) Inparanoid: a comprehensive database of eukaryotic orthologs.Nucleic Acids Res, 33, D476; Wheeler.D.L., Barrett.T., Benson.D.A.,

Bryant.S.H., Canese.K., Chetvernin.V., Church.D.M., DiCuccio.M., Edgar.R.,

Federhen.Set al. (2005) Database resources of the National Center for Biotechnology Information, Nucleic Acids Res, 33, D3; Wood.V. (2006) / Schizosaccharomyces pombe / comparative genomics; from sequence to systems. In Sunnerhagen.P., Piskur.J. (eds.) / Comparative Genomics Using Fungi as Models (Series: Topics in Current Genetics). Vol. 15, pp. 233 and S. Bandyopadhyay, R. Sharan, T. Ideker, Systematic Identification of Functional Orthologs Based on Protein Network Comparison, Genome Res., 16: 428-435 (2006). Most preferably, the orthologous proteins of E1N2 comprise

Amino acid sequences selected from the group consisting of SEQ ID NO: 31, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO : 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 41, SEQ ID NO: 42, SEQ ID NO: 43, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46 , SEQ ID NO: 47, SEQ ID NO: 48, SEQ ID NO: 49, SEQ ID NO: 50, SEQ ID NO: 51, SEQ ID NO: 52 and SEQ ID NO: 53.

The amino acid sequences mentioned are stored in known databases (YDR PDR protein database, UniProt or NCBI (National Center for Biotechnology Information)) under the specified entries:

Table 3: orthologous proteins of EI 2

Organism amino acid sequence deposit

 number (database accession

 No. )

 Arabidopsis thaliana SEQ ID NO: 31 NCBI Reference

 Sequence: NP_195948.1

 Arabidopsis lyrata subsp. SEQ ID NO: 32 NCBI Reference

lyrata sequence:

 XP_002871021.1

 Ricinus communis SEQ ID NO: 33 NCBI Reference

 Sequence:

 XP_002519522.1

 Populus trichocarpa SEQ ID NO: 34 NCBI Reference

 Sequence:

 XP_002322882.1

 Vitis vinifera SEQ ID NO: 35 NCBI Reference

 Sequence:

 XP_002276399.1

 Glycine max SEQ ID NO: 36 NCBI Reference

Sequence: Organism amino acid sequence deposit

 number (database accession

 No. )

 XP_003542536.1

Prunus persica SEQ ID NO: 37 GenBank: ACY78397.1

Cucumis meto SEQ ID NO: 38 GenBank: ADV90799.1

Medicago truncatula SEQ ID NO: 39 NCBI Reference

 Sequence:

 XP_003625647.1

Petunia x hybrida SEQ ID NO: 40 GenBank: AAR08678.1

Solanum lycopersicum SEQ ID NO: 41 NCBI Reference

 Sequence:

 NP_001234518.1

Dianthus caryophyllus SEQ ID NO: 42 GenBank: ADR31357.1

Sorghum bicolor SEQ ID NO: 43 NCBI Reference

 Sequence:

 XP_002457112.1

Zea mays SEQ ID NO: 44 GenBank: AAR25570.1

Oryza sativa Japonica Group SEQ ID NO: 45 GenBank: AAQ95276.1

Oryza sativa Indica Group SEQ ID NO: 46 GenBank: EEC81537.1

Brachypodium distachyon SEQ ID NO: 47 NCBI Reference

 Sequence:

 XP_003575571.1

Triticum aestivum SEQ ID NO: 48 GenBank: ADP02171.1

Malus x domestica SEQ ID NO: 49 GenBank: ABI33219.1

Brassica rapa subsp. SEQ ID NO: 50 GenBank: ADD14032.1 chinensis

 Hordeum vulgare subsp. SEQ ID NO: 51 GenBank: BAJ87351.1 vulgare

 Chlamydomonas reinhardtii SEQ ID NO: 52 NCBI Reference

 Sequence:

 XP_001700793.1

Nicotiana tabacum SEQ ID NO: 53 GenBank: AEI87996.1 More preferably, the orthologous proteins of the ETR1 or its isoforms comprise an amino acid sequence selected from the group consisting of SEQ ID NO: 54, SEQ ID NO: 55, SEQ ID NO: 56, SEQ ID NO: 57, SEQ ID NO : 58, SEQ ID NO: 59, SEQ ID NO: 60, SEQ ID NO: 61, SEQ ID NO: 62, SEQ ID NO: 63, SEQ ID NO: 64, SEQ ID NO: 65, SEQ ID NO: 66 , SEQ ID NO: 67, SEQ ID NO: 68, SEQ ID NO: 69, SEQ ID NO: 70, SEQ ID NO: 71, SEQ ID NO: 72, SEQ ID NO: 73, SEQ ID NO: 74, SEQ ID NO: 75, SEQ ID NO: 76, SEQ ID NO: 77, SEQ ID NO: 78, SEQ ID NO: 79, SEQ ID NO: 80, SEQ ID NO: 81, SEQ ID NO: 82, SEQ ID NO : 83, SEQ ID NO: 84, SEQ ID NO: 85, SEQ ID NO: 86, SEQ ID NO: 87, SEQ ID NO: 88, SEQ ID NO: 89, SEQ ID NO: 90, SEQ ID NO: 91 , SEQ ID NO: 92, SEQ ID NO: 93, SEQ ID NO: 94, SEQ ID NO: 95 and SEQ ID NO: 96. The amino acid sequences mentioned are known in databases (YDR PDR protein database, UniProt or NCBI (National Center for Biotech Nology Information)) under the indicated A lazily deposited:

Table 4: orthologous proteins of ETR1

Organism amino acid sequence deposit

 number (database accession

 No.)

 Arabidopsis lyrata subsp. SEQ ID NO: 54 NCBI Reference

lyrata sequence:

 XP_002887022.1

 Brassica oieracea SEQ ID NO: 7 UniProtKB / Swiss-Prot:

 049230.1

 Dimocarpus longan SEQ ID NO: 11 GenBank: ACL81480.3

 Prunus domestica subsp. SEQ ID NO: 55 GenBank: CAI64505.1 insititia

 Citrus sinensis SEQ ID NO: 8 GenBank: ADB25217.1

Prunus salicina SEQ ID NO: 23 GenBank: ABU68266.1

Prunus persica SEQ ID NO: 21 UniProtKB / Swiss-Prot:

Q9 7M1.1 Organism amino acid sequence deposit

 number (database accession

 No.)

 Popuius trichocarpa ETR4 SEQ ID NO: 56 NCBI Reference

 Sequence:

 XP_002327419.1

Ricinus communis SEQ ID NO: 57 NCBI Reference

 Sequence:

 XP_002533252.1

Fragaria x ananassa SEQ ID NO: 26 GanBank: CAC48384.1

Pyrus communis SEQ ID NO: 58 GenBank: AAL66191.1

Malus x domestica SEQ ID NO: 6 GenBank: AAC31123.1

Pyrus pyrifolia SEQ ID NO: 59 GenBank: BAD61001.1

Populus trichocarpa ETR3 SEQ ID NO: 60 NCBI Reference

 Sequence:

 XP_002299688.1

Actinidia deliciosa ETR1 SEQ ID NO: 61 GenBank: ABY28264.1

Pyrus pyrifolia ETR3 SEQ ID NO: 62 GenBank: ABS57008.1

Coffea canephora SEQ ID NO: 63 GenBank: ABL63474.1

Pelargonium x hortorum SEQ ID NO: 64 UniProtKB / Swiss-Prot: ETR2 Q9XH57.1

 Coffea liberica var. Dewevrei SEQ ID NO: 65 GenBank: ABL63472.1

Mangifera indica SEQ ID NO: 17 GenBank: AAF61919.1

Cucumis melo var. SEQ ID NO: 18 GenBank: AAC99645.1 cantalupensis

 Passiflora edulis SEQ ID NO: 66 UniProtKB / Swiss-Prot:

 Q9ZWL6.1

 Pelargonium x hortorum SEQ ID NO: 13 UniProtKB / Swiss-Prot:

 Q9XH58.1

 Vitis vinrfera SEQ ID NO: 29 NCBI Reference

 Sequence:

 XP_ 002277460.1

Petunia x hybrida SEQ ID NO: 67 GenBank: AAL40901.1 Organism amino acid sequence deposit

 number (database accession

 No.)

 Coffea pseudozanguebariae SEQ ID NO: 68 GenBank: ABL63473.1

Catharanthus roseus SEQ ID NO: 69 GenBank: AAQ10679.1

Ziziphus jujuba SEQ ID NO: 70 GenBanK: ABB77560.1

Cucumis sativus SEQ ID NO: 10 UniProtKB / Swiss-Prot:

 Q9SSY6.1

 Nicotiana tabacum SEQ ID NO: 27 UniProtKB / Swiss-Prot:

 048929.1

 Solanum lycopersicum SEQ ID NO: 71 UniProtKB / Swiss-Prot:

 Q41342.1

 Medicago truncatula SEQ ID NO: 72 NCBI Reference

 Sequence:

 XP_003605421.1

Hevea brasiliensis SEQ ID NO: 14 GenBank: AAW31759.1

Diospyros kaki SEQ ID NO: 12 GenBank: BAE46932.1

Glycine max SEQ ID NO: 25 GenBank: ABR67685.1

Lactuca sativa SEQ ID NO: 16 GenBank: AAQ15122.1

Solanum lycopersicum ETR2 SEQ ID NO: 73 NCBI Reference

 Sequence:

 NP_001234153.1

Eriobotrya japonica SEQ ID NO: 74 GenBank: ACM89298.1

Lilium formosanum x Lilium SEQ ID NO: 75 GenBank: ABD66593.1 longiflorum

 Musa acuminata AAA Group SEQ ID NO: 76 GenBank: AAQ13533.1

Gladiolus hybrid cultivar SEQ ID NO: 77 GenBank: BAD20704.1

Papilionanthe hookeriana x SEQ ID NO: 78 GenBank: AEE69544.1 Papilionanthe teres

 Oncidium Gower Ramsey SEQ ID NO: 79 GenBank: AAQ14309.1

Phalaenopsis hybrid cultivar SEQ ID NO: 80 GenBank: AAD04949.1 ERS

Dendrobium hybrid cultivar SEQ ID NO: 81 GenBank: ABJ91124.1 Organism amino acid sequence deposit

 number (database accession

 No.)

 Phalaenopsis hybrid cultivar SEQ ID NO: 82 GenBank: AAD26899.1

Phalaenopsis equestris SEQ ID NO: 83 GenBank: CAD91247.1

Sorghum bicolor SEQ ID NO: 84 NCBI Reference

 Sequence:

XP _. 002464032.1

 Dendrobium hybrid cultivar SEQ ID NO: 85 GenBank: ACN22272.1

Oryza sativa Japonica Group SEQ ID NO: 19 GenBank: ABF98411.1

Oryza sativa SEQ ID NO: 86 GenBank: AAB72193.1

Hordeum vulgare subsp. SEQ ID NO: 87 GenBank: BAJ87109.1 vulgare

 Zea mays SEQ ID NO: 88 GenBank: AAR25566.1

Saccharum hybrid cultivar SEQ ID NO: 89 GenBank: ADJ66722.1 ROC20

 Delphinium 'MagicFountains SEQ ID NO: 90 GenBank: BAB84569.1 dark blue'

 Triticum aestivum ERS SEQ ID NO: 91 GenBank: ADJ67795.1

Triticum aestivum ERS3 SEQ ID NO: 92 GenBank: ADK23798.2

Triticum aestivum ERS2 SEQ ID NO: 93 GenBank: ADK23797.2

Delphinium x belladonna SEQ ID NO: 94 GenBank: BAD89291.1

Actinidia deliciosa ERS1 SEQ ID NO: 95 GenBank: ABY28263.1

Populus trichocarpa SEQ ID NO: 96 NCBI Reference

 Sequence:

 XP_002302732.1

In the ethylene tag label, the receptor protein ETR1 or its isoform ERS1, ETR2, ERS2, EIN4 or a homologous or orthologous protein thereof interacts with the EIN2 protein. The region of the amino acid sequence of the ETR1 or its isoforms ERS1, ETR2, ERS2, EIN4, or a homologous or orthologous protein thereof which interacts with the EIN2 or an orthologous protein thereof is described in U.S. Pat This is occasionally also referred to as the contact domain of the ETRi which interacts with EIN2 or an orthologous protein thereof, or even just as the contact domain of the ETRi

ETR1 designates. Plants and / or their fruits

The plants of the method according to the invention are preferably selected from the group consisting of useful plants and ornamental plants. Their fruits are correspondingly preferably selected from the group consisting of the fruits of crops and ornamental plants.

The term crops as used herein refers to crops used as plants for the production of food, feed, fuel or for technical purposes. Ornamental plants are understood to be, in particular, annual and perennial plants such as cut flowers and / or their plant extracts.

Preferably, the crops are selected from the group of the following

Plant species: triticale, durum (durum wheat), turf, vines, cereals, such as wheat, barley, rye, oats, rice, corn and millet; Beets, for example

Sugar beets and fodder beets; Fruits, such as pome fruit, stone fruit and

 Berry fruits, such as apples, pears, plums, peaches, almonds, cherries and berries, eg. Strawberries, raspberries, blackberries or even mango, dates and figs; Legumes, such as beans, lentils, peas and soybeans;

Oil crops, such as oilseed rape, mustard, poppy, olives, sunflowers, coconut,

Castor oil plants, cocoa beans and peanuts; Cucurbits, for example squash, cucumbers and melons; Fiber plants, for example cotton, flax, hemp and jute; Citrus fruits, such as oranges, lemons, grapefruit and mandarins; Vegetables such as spinach, (head) salad, asparagus, cabbages, carrots, onions, tomatoes, potatoes and peppers; Laurel family, such as avocado, cinnamomum, camphor, or plants such as tobacco, nuts, coffee, eggplant, sugar cane, tea, pepper, vines, hops, bananas,

Natural rubber plants and ornamental plants, such as flowers and shrubs. This list is not a limitation. As a particularly suitable target cultures for the application of the invention

Oats, rye, triticale, durum, cotton, aubergine, turf, pome fruit, stone fruit, soft fruit, maize, wheat, barley, cucumber, tobacco, vines, rice, cereals, pear, pepper, beans, soybeans, Rapeseed, tomato, paprika, melons, cabbage, potato and apple.

As cut flowers and / or their plant parts, which after the

For example, roses, carnations, gerberas, lilies, daisies, chrysanthemums, tulips, daffodils, anemones, poppies, amyrillis, dahlias, azaleas, mallows, but also e.g. bedding plants,

Potted plants and perennials, such as roses, tagetes, pansies, geraniums, fuchsias, hibiscus, chrysanthemums, hardy lits, cyclamen, southern violets, sunflowers, begonias. In one embodiment of the method according to the invention, the plants are transgenic plants.

Particularly preferably, the transgenic plants can be selected from the group consisting of herbicide-tolerant plants, insect-resistant plants, plants with increased stress tolerance, plants, which altered the amount, quality and / or shelf life of the harvested product and / or altered

Have properties of certain components of the harvested product, plants with altered fiber properties and plants with altered

Oil saturation.

Plants or plant varieties (obtained by plant biotechnology methods, such as genetic engineering) which can be used in the process according to the invention are herbicidally tolerant plants, ie plants which have been made tolerant to one or more given herbicides. Such plants can be obtained either by genetic transformation or by selection of plants containing a mutation conferring such herbicide tolerance. Herbicide-tolerant plants are, for example, glyphosate-tolerant plants, ie

Plants _»that have been made tolerant to the herbicide glyphosate or salts thereof. For example, glyphosate-tolerant plants can be obtained by transforming the plant with a gene encoding the enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS). Examples of such EPSPS genes are the AroA gene (mutant CT7) of the bacterium Salmonella typhimurium (Comai et al., Science (1983), 221, 370-371), the GP4 gene of the bacterium

Agrobacterium sp. (Barry et al., Curr Topics Plant Physiol., (1992), 7, 139-145), the genes responsible for petunia EPSPS (Shah et al., Science (1986), 233, 478-481). , for a EPSPS from the tomato (Gasser et al., J. Biol. Chem. (1988), 263, 4280- 4289) or for an EPSPS from Eleusine (WO 01/66704) encode. It may also be a mutated EPSPS, as described for example in EP-A 0837944, WO

00/066746, WO 00/066747 or WO 02/026995. Glyphosate-tolerant plants can also be obtained by expressing a gene coding for a glyphosate oxidoreductase enzyme as described in US 5,776,760 and US 5,463,175. Glyphosate-tolerant plants may also be obtained by expressing a gene encoding a glyphosate acetyltransferase enzyme as described in, e.g. WO 02/036782, WO 03/092360, WO 05/012515 and WO 07/024782. Glyphosate-tolerant plants can also be obtained by culturing plants containing the naturally occurring mutations of the above-mentioned genes, as described, for example, in WO 01/024615 or WO

03/013226 are described, contained, selected.

Other herbicide-resistant plants are, for example, plants which have been tolerated to herbicides which inhibit the enzyme glutamine synthase, such as bialaphos, phosphinotricin or glufosinate. Such plants can be obtained by expressing an enzyme which detoxifies the herbicide or a mutant of the enzyme glutamine synthase, which is resistant to inhibition. Such an effective detoxifying enzyme is, for example, an enzyme suitable for

Phosphinotricin acetyltransferase encoded (such as the bar or pat protein from Streptomyces species). Plants expressing an exogenous phosphinotricin acetyltransferase are described, for example, in US 5,561,236; US 5,648,477; US 5,646,024; US 5,273,894; US 5,637,489; US 5,276,268; US 5,739,082; US 5,908,810 and US 7,112,665. Further herbicide-tolerant plants are also plants tolerant to the herbicides which inhibit the enzyme hydroxyphenylpyruvate dioxygenase (HPPD). The hydroxyphenylpyruvate dioxygenases are enzymes that catalyze the reaction in which para-hydroxyphenylpyruvate (HPP) is converted to homogentisate. Plants tolerant of HPPD inhibitors may be treated with a gene encoding a naturally occurring resistant HPPD enzyme, or a gene encoding a mutant HPPD enzyme as described in WO 96/038567, WO 99/024585 and WO 99/1998 / 024586, are transformed. Tolerance to HPPD inhibitors can also be achieved by transforming plants with genes encoding certain enzymes that allow the formation of homogentisate despite inhibition of the native HPPD enzyme by the HPPD inhibitor. Such plants and genes are described in WO 99/034008 and WO 2002/36787. The tolerance of plants to HPPD inhibitors can also be improved by transforming plants, in addition to a gene which codes for an HPPD-to-oxidant enzyme, with a gene which codes for a prephenate dehydrogenase enzyme, as described in WO 2004 / 024928 is described.

Other herbicide-resistant plants are plants that have been tolerated to acetolactate synthase (ALS) inhibitors. Examples of known ALS inhibitors include sulfonylurea, imidazolinone, triazolopyrimidines,

Pyrimidyloxy (thio) benzoates and / or sulfonylaminocarbonyl-triazolinone herbicides. It is known that various mutations in the enzyme ALS (also known as

Acetohydroxy acid synthase, AHAS, known) a tolerance to

different herbicides or groups of herbicides, as described, for example, by Tranel and Wright, Weed Science (2002), 50, 700-712, but also in US Pat. Nos. 5,605,011, 5,378,824, 5,141,870 and 5,013,659. is described. The production of sulfonylurea tolerant plants and imidazolinone tolerant

Plants is described in US 5,605,011; US 5,013,659; US 5,141,870; US 5,767,361; US

5,731,180; US 5,304,732; US 4,761,373; US 5,331, 107; US 5,928,937; and US

 5,378,824; and in international publication WO 96/033270. Other imidazolinontolerante plants are also in z. WO 2004/040012, WO

2004/106529, WO 2005/020673, WO 2005/093093, WO 2006/007373, WO

2006/015376, WO 2006/024351 and WO 2006/060634. Further Sulfonylurea and imidazolinone tolerant plants are also in, for example, WO

 2007/024782 described.

Other plants that are resistant to ALS inhibitors, especially against

Imidazolinones, sulfonylureas and / or sulfamoylcarbonyltriazolinones, can be obtained by induced mutagenesis, selection in cell cultures in the presence of the herbicide or by mutation breeding, as for example for the soybean in US 5,084,082, for rice in WO 97/41218, for Sugar beet in US 5,773,702 and WO 99/057965, for salad in US 5,198,599 or for the sunflower in WO 2001/065922 is described.

Plants or plant varieties (obtained by plant biotechnology methods such as genetic engineering), which may also be used in the method of the invention, are insect-resistant transgenic plants, i. Plants that have been made resistant to attack by certain target insects. Such plants can be obtained by genetic transformation or by selection of plants containing a mutation conferring such insect resistance.

The term "insect-resistant transgenic plant" as used herein

Relates to any plant containing at least one transgene comprising a coding sequence coding for:

1) an insecticidal crystal protein from Bacillus thuringiensis or an insecticidal portion thereof, such as the insecticidal crystal proteins collected by Crickmore et al., Microbiology and Molecular Biology Reviews (1998), 62, 807-813, by Crickmore et al. (2005) in the Bacillus thuringiensis toxin nomenclature (online at: http: //www.lifesci.suspsex.ac.uk/Home/NeiLCrickmore/Bt/), or insecticidal portions thereof, e.g. Proteins of the cry protein classes CrylAb, CrylAc, Cry1F, Cry2Ab, Cry3Ae or Cry3Bb or insecticidal parts thereof; or

2) a crystal protein from Bacillus thuringiensis or a part thereof, in the presence of a second, other crystal protein than Bacillus thuringiensis or a part thereof insecticidal, such as the binary toxin consisting of the crystal proteins Cy34 and Cy35 (Moellenbeck et al., Nat. Biotechnol. (2001), 19, 668-72; Schnepf et al., Applied Environment Microb. (2006) , 71, 1765-1774); or 3) an insecticidal hybrid protein comprising parts of two different insecticides of Bacillus thuringiensis crystal proteins, such as a hybrid of the proteins of 1) above or a hybrid of the proteins of 2) above, e.g. For example, the protein Cry1A.105 produced by the corn event MON98034 (WO

2007/027777); or

4) a protein according to any one of items 1) to 3) above, in which some, in particular 1 to 10, amino acids have been replaced by another amino acid to achieve a higher insecticidal activity against a target insect species and / or the spectrum of the corresponding Extend target species and / or because of

Changes induced in the coding DNA during cloning or transformation, such as the protein Cry3Bb1 in maize events MON863 or MON88017 or the protein Cry3A in the maize event MIR 604; or

5) an insecticidal secreted protein from Bacillus thuringiensis or Bacillus cereus or an insecticide part thereof, such as the insecticidal insectivorous

Proteins (vegetative insecticidal proteins, VIP), which are listed under the following link, for. B. Proteins of protein class VIP3Aa:

or 6) a secreted protein from Bacillus thuringiensis or Bacillus cereus, which acts in the presence of a second secreted protein from Bacillus thuringiensis or B. cereus insecticide, such as the binary toxin consisting of the proteins VIP1A and VIP2A (WO 94/21795); or 7) an insecticidal hybrid protein comprising parts of various secreted proteins of Bacillus thuringiensis or Bacillus cereus, such as a hybrid of the proteins of 1) or a hybrid of the proteins of 2) above; or 8) a protein according to any of items 1) to 3) above, in which some, in particular 1 to 10, amino acids have been replaced by another amino acid in order to achieve a higher insecticidal activity against a target insect species and / or the spectrum of the corresponding Extend target species and / or because of

Changes induced in the coding DNA during cloning or transformation (preserving the coding for an insecticidal protein), such as protein VIP3Aa in cotton event COT 102.

Of course, insect-resistant transgenic plants in the present context also include any plant comprising a combination of genes encoding the proteins of any of the above classes 1 to 8. In one embodiment, an insect resistant plant contains more than one transgene encoding a protein of any one of the above 1 to 8 in order to extend the spectrum of the corresponding target insect species or to develop a protein

To delay insect resistance to plants by using different proteins which are insecticidal for the same target insect species, but a different mode of action, such as binding to different ones

Receptor binding sites in the insect. Plants or plant varieties (obtained by methods of plant biotechnology, such as genetic engineering), which can also be used in the method according to the invention, are tolerant of abiotic stress factors.

Such plants can be obtained by genetic transformation or by selection of plants containing a mutation conferring such stress resistance. Particularly useful plants with stress tolerance include the following: a. Plants which contain a transgene which have the expression and / or activity of the gene for the poly (ADP-ribose) polymerase (PARP) in the plant cells or

To reduce plants, as described in WO 2000/004173 or EP 04077984.5 or EP 06009836.5. (b) plants containing a stress tolerance enhancing transgene capable of reducing the expression and / or activity of the PARP-encoding genes of the plants or plant cells, as described, for example, in WO 2004/090140; 80 c.Plants containing a stress tolerance-enhancing transgene encoding a plant-functional enzyme of the nicotinamide adenine dinucleotide salvage biosynthetic pathway, including nicotinamidase, nicotinate phosphoribosyltransferase,

Nicotinsäuremononukleotid-adenyltransferase,

 Nicotinamide adenine dinucleotide synthetase or nicotinamide phosphoribosyltransferase as described e.g. As described in EP 04077624.7 or WO 2006/133827 or PCT / EP07 / 002433. Plants or varieties of plants (which have been obtained by methods of plant biotechnology, such as genetic engineering), which can also be used in the method according to the invention, have a modified amount, quality and / or

Shelf life of the crop and / or altered characteristics of certain components of the crop, such as:

1) Transgenic plants that synthesize a modified starch with respect to their physicochemical properties, in particular the amylose content or the amyiose / amylopectin ratio, the degree of branching, the average chain length, the distribution of the side chains, the viscosity behavior, the

Gel strength, the starch grain size and / or starch grain morphology is changed in comparison with the synthesized starch in Wiidtyppflanzenzellenzellen or plants, so that this modified starch is better suited for certain applications. These transgenic plants which synthesize a modified starch are described, for example, in EP 0571427, WO 95/004826, EP 0719338, WO 96/15248, WO 96/19581, WO

96/27674, WO 97/1 1188, WO 97/26362, WO 97/32985, WO 97/42328, WO 97/44472, WO 97/45545, WO 98/27212, WO 98/40503, WO 99/58688, WO 99/58690, WO 99/58654, WO 2000/008184, WO 2000/008185, WO 2000/28052, WO 2000/77229, WO 2001/12782, WO 2001/12826, WO 2002/101059, WO 2003/071860, WHERE

2004/056999, WO 2005/030942, WO 2005/030941, WO 2005/095632, WO

2005/095617, WO 2005/095619, WO 2005/095618, WO 2005/123927, WO

2006/018319, WO 2006/103107, WO 2006/108702, WO 2007/009823, WO

WO 00/029030, WO 2006/033862, WO 2006/072603, WO 2002/034923, EP 06090134.5, EP 06090228.5, EP 06090227.7, EP 07090007.1, EP 07090009.7, WO 2001/14569, WO 2002/79410, WO 2003/33540, WO 2004/078983, WO 2001/19975, WO 95/26407, 81

 WO 96/34968, WO 98/20145, WO 99/12950, WO 99/66050, WO 99/53072, US Pat. No. 6,734,341, WO 2000/11192, WO 98/22604, WO 98/32326, WO 2001/98509, WO 2001 / 98509, WO 2005/002359, US 5,824,790, US 6,013,861, WO 94/004693, WO 94/009144, WO 94/11520, WO 95/35026 and WO 97/20936, respectively.

2) Transgenic plants that synthesize non-starch carbohydrate polymers or non-starch carbohydrate polymers, whose properties are comparable to

Wildtype plants are modified without genetic modification. Examples are plants which produce polyfructose, in particular of the inulin and levan type, as described in EP 0663956, WO 96/001904, Wo 96/021023, WO 98/039460 and WO 99/024593, plants which are alpha-1 To produce 4-glucans, as in WO

95/031553, US 2002/031826, US 6,284,479, US 5,712,107, WO 97/047806, WO 97/047807, WO 97/047808 and WO 2000/14249, plants which are alpha-1, 6-branched alpha-1 4-glucans, as described in WO 2000/73422

and plants which produce alternan, as described in WO 2000/047727, EP 06077301.7, US 5,908,975 and EP 0728213.

3) Transgenic plants which produce hyaluronan, as described, for example, in WO 06/032538, WO 2007/039314, WO 2007/039315, WO 2007/039316, JP 2006/304779 and WO 2005/012529.

Plants or plant varieties (obtained by plant biotechnology methods, such as genetic engineering), which can also be used in the method according to the invention, are plants such as cotton plants with altered fiber properties. Such plants can be obtained by genetic transformation or by selection of plants containing a mutation conferring such altered fiber properties; These include: a) plants, such as cotton plants, which have an altered form of

Cellulose synthase genes, as described in WO 98/000549, b) plants, such as cotton plants, which contain an altered form of rsw2 or rsw3-homologous nucleic acids, as described in WO 2004/053219; c) plants such as cotton plants with an increased expression of the

Sucrose phosphate synthase as described in WO 2001/017333; d) plants such as cotton plants with an increased expression of

Sucrose synthase as described in WO 02/45485; e) plants such as cotton plants in which the timing of the passage control of the Plasmodesmen is changed at the base of the fiber cell, z. B. by

Downregulating the fiber-selective β-1,3-glucanase as described in WO 2005/017157; f) plants such as cotton plants with modified reactivity fibers, e.g. By expression of the N-acetylglucosamine transferase gene, including nodC, and chitin synthase genes, as described in WO 2006/136351.

Plants or plant varieties (obtained by plant biotechnology methods such as genetic engineering) which can also be used in the method according to the invention are plants such as rapeseed or related Brassica plants with altered properties of the oil composition. Such plants can be obtained by genetic transformation or by selection of plants containing a mutation conferring such altered oil properties; These include: a) plants such as rape plants that produce high oleic acid oil, as described, for example, in US 5,969,169, US 5,840,946 or US 6,323,392 or US 6,063,

947 is described; b) plants such as oilseed rape plants which produce low linolenic acid oil, as described in US 6,270,828, US 6,169,190 or US 5,965,755. c) plants such as oilseed rape plants which produce oil with a low saturated fatty acid content, such as e.g. As described in US 5,434,283. Particularly useful transgenic plants that may find application in the method of the invention are plants that contain transformation events, or a combination of transformation events, and that are listed, for example, in the files of various national or regional authorities.

YIELD GARD ^® (for example maize: Particularly useful transgenic plants which may be used in the present process are exemplary plants with one or more genes that encode one or more toxins are the transgenic plants which are sold under the following trade names , cotton, soya beans), KnockOut ^® (for example maize), BiteGard ^® (for example maize), BT-Xtra ^® (for example maize), StarLink ^® (for example maize), Bollgard ^® (cotton), NuCOTN ^® (cotton ), NuCOTN ^® 33B (cotton), NatureGard® ^® (for example maize), Protecta ^® and Ne Leaf ^® (potato). Herbicide-tolerant plants to be mentioned are, for example, maize varieties, cotton varieties and

Soybean varieties sold under the following tradenames: Roundup ^Ready® (glyphosate tolerance, for example corn, cotton, soybean), Liberty ^Link® (phosphinotricin tolerance, for example rapeseed), ^IMI®

(Imidazolinone) and SCS ^® (Sylfonylharnstofftoleranz), for example, maize. To the herbicide-resistant plants (traditionally grown on herbicide tolerance

Plants) that may be mentioned include the varieties sold under the name Clearfield ^® (for example maize).

Treatment of the plants and / or their fruits The plants and / or their fruits are particularly preferred

Process according to the invention treated with the interaction inhibiting compound for influencing their maturation process, their senescence process and / or their stress tolerance. The term "treatment" includes all measures that lead to contact between these agents and at least one

Plant or fruit part lead.

The interaction-inhibiting compound of the present invention can be formulated in various ways, depending on which biological and / or chemical

physical parameters are given. As formulation options come for example: wettable powders (WP), water-soluble powders (SP), water-soluble concentrates, emulsifiable concentrates (EC), emulsions (EW), such as oil in water and water in oil emulsions, sprayable solutions, suspension concentrates (SC), dispersions on oil or water-based, oil-miscible solutions, capsule suspensions (CS), dusts (DP), mordants, granules for litter application, granules (GR) in the form of micro, spray, elevator and adsorption granules,

water-dispersible granules (WG), water-soluble granules (SG), ULV

Formulations, microcapsules and waxes. These individual formulation types are known and will be known in principle

for example described in: Winnacker Küchler, "Chemical Technology",

Volume 7, C. Hanser Verlag Munich, 4th ed. 1986; Wade van Valkenburg, "Pesticide Formulations", Marcel Dekker, N.Y., 1973; K. Martens, "Spray Drying" Handbook, 3rd ed. 1979, G. Goodwin Ltd. London.

The necessary wording help center! inert materials, surfactants, solvents, auxiliaries and other additives are also known and are described, for example, in Watkins, Handbook of Insecticides Dust Diluents and Carriers, 2nd ed., Darland Books, Caldwell N.J., H.v. Olphen, "Introduction to Clay Colloid

Chemistry; 2nd Ed., J. Wiley & Sons, NY; C. Marsden, "Solvent Guide"; 2nd Ed., Interscience, NY 1963; McCutcheon's "Detergents and Emulsifiers Annual", MC Publ. Corp., Ridgewood NJ; Sisley and Wood, "Encyclopedia of Surface Active Agents", Chem. Publ. Co. Inc., NY 1964; Schonfeldt, "Grenzflächenaktive

Äthylenoxidaddukte ", Wiss. Verlagsgesell., Stuttgart 1976; Winnacker Küchler,

"Chemical Technology", Volume 7, C. Hanser Verlag Munich, 4th ed. 1986.

Injectable powders are preparations which are uniformly dispersible in water and contain not only the interaction-inhibiting compound but also surfactants of an ionic and / or non-ionic type (wetting agent, dispersing agent), e.g.

polyoxyethylated alkylphenols, polyoxethylated fatty alcohols, polyoxethylated

Fatty amines, fatty alcohol polyglycol ether sulfates, alkanesulfonates, alkylbenzenesulfonates, lignosulfonate sodium, 2,2 'dinaphthylmethane, 6,6' disulfonic acid sodium, dibutylnaphthalene sulfonic acid sodium or oleoylmethyltaurine acid. To prepare the wettable powders, the interaction inhibits Compounds, for example, in conventional apparatus such as hammer mills,

Fan mills and air jet mills finely ground and at the same time or

then admixed with the formulation aids. Dusts are obtained by milling the interaction inhibiting compound with finely divided solids, e.g. Talc, natural clays such as kaolin, bentonite and pyrophyllite, or diatomaceous earth.

Suspension concentrates may be water or oil based. You can

for example, by wet grinding by means of commercially available bead mills and, if appropriate, addition of surfactants, as described, for example, in US Pat. above at the other

Formulation types already listed are produced.

Emulsions, e.g. Oil-in-water emulsions (EW) can be prepared, for example, by means of stirrers, colloid mills and / or static mixers using aqueous organic solvents and optionally surfactants such as those described e.g. listed above for the other formulation types.

Granules can either inhibit by inhibiting the interaction

Compound be made on adsorptive, granulated inert material or by applying concentrates by means of adhesives, e.g. Polyvinyl alcohol, sodium poliyacrylic or mineral oils, on the surface of carriers such as sand, kaolinites or granulated inert material. Water-dispersible granules are generally prepared by the usual methods such as spray-drying, fluidized-bed granulation, plate granulation, mixing with high-speed mixers and extrusion without solid inert material.

For the preparation of plates, fluidized bed, extruders and spray granules, see e.g.

Process in "Spray Dryirtg Handbook" 3rd ed. 1979, G. Goodwin Ltd., London; JE Browning, "Agglomeration", Chemical and Engineering 1967, pages 147 ff .; Perry's Chemical Engineer's Handbook, 5th Ed., McGraw Hill, New York 1973, p. 8 57. The preparations according to the invention generally contain from 0.1 to 99% by weight, in particular from 0.1 to 95% by weight, of the compound inhibiting the interaction. In

Spray powders, the concentration is e.g. about 10 to 90% by weight, the remainder to 100% by weight consists of customary formulation constituents. When emulsifiable

Concentrates may be the concentration of the interaction inhibiting compound about 1 to 90, preferably 5 to 80 wt.%. Dust-like formulations contain from 1 to 30% by weight of the interaction-inhibiting compound, preferably most often from 5 to 20% by weight of the interaction-inhibiting compound. Sprayable solutions contain from about 0.05 to 80, preferably from 2 to 50% by weight of the

Interaction inhibiting compound. In the case of water-dispersible granules, the content of the compound inhibiting the interaction depends, in part, on whether the active compound is liquid or solid and which granulation aid!

Fillers, etc. are used. In the case of the water-dispersible granules, the content of the interaction-inhibiting compound is, for example, between 1 and 95% by weight, preferably between 10 and 80% by weight.

In addition, the formulations mentioned optionally contain the customary adhesive, wetting, dispersing, emulsifying, penetrating, preserving, antifreezing and solvent, filling, carriers and dyes, antifoams, evaporation inhibitors and the pH and viscosity-influencing agents.

In a preferred embodiment, the interaction inhibiting compound is applied in the form of an aqueous solution in the plants and / or fruits on the surface of the plants and / or fruits.

Further preferably, the interaction-inhibiting compound is sprayed or applied to the surface of the plants and / or fruits or that the plants and / or fruits are immersed in the aqueous solution of the interaction-inhibiting compound. Particularly preferred is the interaction

inhibiting compound used in the form of an aqueous solution.

The present invention therefore further relates to a spray formulation of the interaction inhibiting compound for influencing the ripening process, the senescence process and / or the stress tolerance of plants and / or their fruits. In the following, a spray formulation is described in more detail:

The formulations for spray application are prepared in a known manner, e.g. by mixing the invention to be used, the interaction

inhibiting compound with extenders _"that is liquid solvents and / or solid carriers, optionally with the use -of surfactants, that is emulsifiers and / or dispersants and / or foam-forming agents. Further customary additives, such as, for example, customary extenders and solvents or diluents, dyes, wetting agents, dispersants,

 Emulsifiers, defoamers, preservatives, secondary thickeners, adhesives, gibberellins, and also water may optionally be used. The preparation of the formulations is carried out either in suitable systems or before or during use.

Excipients which can be used are those which are suitable for imparting special properties to the composition itself or to preparations derived therefrom (for example spray mixtures), such as certain technical properties and / or special biological properties. As typical aids are:

Extenders, solvents and carriers.

As a diluent is particularly suitable water. As a wetting agent in the

All formulations which can be used according to the invention may contain all wetting-promoting substances customary for the formulation of agrochemical active compounds. Preferably used are alkylnaphthalene sulfonates, such as

Diisopropyl or diisobutylnaphthalene sulfonates.

Suitable dispersants and / or emulsifiers which may be present in the formulations which can be used according to the invention are all nonionic, anionic and cationic dispersants which are customary for the formulation of agrochemical active compounds. Preferably usable are nonionic or anionic dispersants or mixtures of nonionic or anionic dispersants. Particularly suitable nonionic dispersants are ethylene oxide-propylene oxide block polymers, alkylphenol polyglycol ethers and tristryrylphenol polyglycol ethers and their phosphated or sulfated derivatives.

 Suitable anionic dispersants are in particular lignosulfonates,

 Polyacryic acid salts and arylsulfonate-formaldehyde condensates.

Defoamers which may be present in the formulations which can be used according to the invention are all foam-inhibiting substances customary for the formulation of agrochemical active compounds. Preferably usable are silicone defoamers and

 Magnesium stearate.

As preservatives can be used in the invention

 Formulations all substances that can be used for such purposes in agrochemical agents be present.

Suitable secondary thickeners which may be present in the formulations which can be used according to the invention are all substances which can be used for such purposes in agrochemical compositions. Preference is given to cellulose derivatives, acrylic acid derivatives, xanthan, modified clays and finely divided

Silica.

Suitable adhesives which may be present in the formulations which can be used according to the invention are all customary binders which can be used in pickling agents.

Preferably mentioned are polyvinylpyrrolidone, polyvinyl acetate, polyvinyl alcohol and Tylose.

More valuable additives may be fragrances, mineral or vegetable optionally modified oils, waxes and nutrients (also trace nutrients), such as salts of iron, manganese, boron, copper, cobalt, molybdenum and zinc. Stabilizers such as cold stabilizers, antioxidants, light stabilizers or other chemical and / or physical stability improving agents may also be included.

The formulations generally contain between 0.01 and 98% by weight, preferably between 0.5 and 90%, of the interaction inhibiting compound. 89

 In a further aspect of the present invention there is provided a means for influencing the ripening process, the senescence process and / or the stress tolerance of plants and / or their fruits comprising at least one compound selected from the group consisting of a peptide, a peptide mimetic, an aptamer, an antibody and / or its fragments, characterized in that the peptide or antibody and / or its fragments comprises an amino acid sequence selected from the group consisting of the amino acid sequence SEQ ID NO: 1, the

Amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, that the

Peptide mimetic comprises at least one backbone modified amino acid sequence selected from the group consisting of

Amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3 or that the aptamer is prepared on the basis of the target structure of a peptide, wherein the peptide is selected from the amino acid sequence SEQ ID NO: 1, the amino acid sequence

 SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of

Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of

 Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3. In this case, compounds are excluded in which the peptide and / or the antibody and / or its

Fragments an amino acid sequence of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 or SEQ ID NO: 102, and / or a part of one of Amino acid sequences SEQ ID NO: 98 to SEQ ID NO: 102, which comprises at least 6 of the amino acids mentioned in SEQ ID NO: 98 to SEQ ID NO: 102 and / or comprises a derivative of the amino acid sequences SEQ ID NO: 98 to 102 and / or in which a peptide mimetic is modified from a backbone on the peptide

Amino acid sequence which is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 102, and / or in which an aptamer Based on the target structure of a peptide, wherein the peptide is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100 SEQ ID NO: 101 and SEQ ID NO: 102.

Likewise, a means for influencing the maturation process, the

Senescence process and / or the stress tolerance of plants and / or their fruits provided at least one compound which is selected from the group consisting of a peptide, a peptide mimetic, an aptamer, an antibody and / or its fragments, characterized in that Peptide or the antibody and / or fragments thereof has the amino acid sequence SEQ ID NO: 103, a part of the amino acid sequence SEQ ID NO: 103 which comprises at least 4, preferably at least 5, particularly preferably at least 6 of the amino acids mentioned in SEQ ID NO: 102, or a derivative of the amino acid sequence SEQ ID NO: 103, the peptide mimetic comprises the peptide backbone modified amino acid sequence of SEQ ID NO: 103, a part of the peptide backbone

modified amino acid sequence SEQ ID NO: 103, which comprises at least 4, preferably at least 5, more preferably at least 8 of the amino acids mentioned in SEQ ID NO: 103, or a derivative of a peptide backbone modified

 Amino acid sequence SEQ ID NO: 103 or that the aptamer is prepared on the basis of the target structure of a peptide, the peptide being selected from the amino acid sequence SEQ ID NO: 103, a part of one of the amino acid sequences SEQ ID NO: 103, which is at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 103, and a derivative of the amino acid sequence SEQ ID NO: 103, wherein, when the

Amino acid sequence SEQ ID NO: 103 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 103 is alanine. This agent can also comprise the above-described preferred embodiments of the compounds which are selected from the group consisting of the peptide according to the invention, the antibody according to the invention and / or its fragments, the peptide mimetic according to the invention, the aptamer according to the invention and combinations of these compounds according to the invention.

In particular, the agent is characterized in that it is the interaction of the protein EIN2 (Ethylene Insensitive 2) or an orthologous protein thereof with the receptor protein ETR1 (Ethylene resistant 1), its isoforms ERS1, ETR2, ERS2, EIN4 or homologous or orthologous proteins thereof by interacting with a contact domain of the ethylene receptor ETR1 or its isoforms ERS1, ETR2, ERS2, EIN4 or a homologous or orthologous protein thereof.

In a preferred embodiment, the agent comprises at least one further compound which is suitable for influencing the ripening process, the senescence process and / or the stress tolerance of plants and / or their fruits. It is preferably an ethylene antagonist.

In a further preferred embodiment, the agent additionally comprises at least one formulating agent which is selected from the group consisting of inert materials, surfactants, solvents and auxiliaries.

PREFERRED EMBODIMENTS Embodiment 1: Method for Influencing the Ripening Process,

Senescence process and / or the stress tolerance of plants and / or their

Fruits, characterized in that in the plants and / or fruits the

Interaction of the protein EIN2 (Ethylene Insensitive 2) or an orthologous protein thereof with the receptor protein ETR1 (Ethylene resistant 1) of its isoforms ERS1, ETR2, ERS2, EIN4 or homologous or orthologous proteins thereof by the

Interaction of a compound selected from the group consisting of a peptide, a peptide mimetic and mixtures of these compounds with a contact domain of the ethylene receptor ETR1 or its isoforms ERS1, ETR2, ERS2, EIN4 or a homologous or orthologous protein thereof is inhibited, wherein the contact domain is that which interacts with EIN2 or an orthoiogenic protein thereof.

Description of the pictures

Figure 1: Representation of species having a protein homologous to ETR1, partially indicating the degree of agreement

Figure 2: Results of Example 1: Determination of in vitro ETR1-EIN2 interaction based on tryptophan fluorescence by the addition of NLSOP-1 (peptide capable of interacting with the contact domain of ETR1) and ROP-1 {Peptide with random amino acid sequence _» as a control)

FIG. 3: Results of Example 2: Determination of the ETA1 and mCherry Labeled ETR1 in Planta FRET Efficiency of a GFP with Addition of NLSOP-1 (Peptide Capable of Interacting with the Contact Domain of the ETR1) and ROP-1 (FIG. Peptide with random amino acid sequence, as a control)

Figure 4: Results of Example 3: the determination of the hypocotyl length of

 Arabidopsis using NLSOP-1 at different concentrations (peptide capable of interacting with the contact domain of ETR1) and ROP-1 (random amino acid peptide, control); * means: P <0.005 compared to positive control (ACC only)

FIG. 5: Results of Example 5: Determination of the in vitro ETR1 -EIN2 interaction on the basis of the FRET efficiency of an Alexa Fluor 568-labeled EIN2 ^{479 "1297} and an Alexa Fluor 488-labeled ETR1 with the addition of different peptides

FIG. 6: Results of Example 6: Determination of the in vitro ETR1-EIN2 interaction on the basis of the FRET efficiency of an Alexa Fluor 568-labeled E1N2 ^{479 "1297} and an Alexa Fluor 488-labeled ETR1 with the addition of different sequence variants of the peptide SEQ ID NO: 4

FIG. 7: Results of example 7: Determination of the in vitro ETR1-E1N2 interaction on the basis of the FRET efficiency of an Alexa Fluor 568-labeled E1 2 ^{479 "1297} and an Alexa Fluor 488-labeled ETR1 with the addition of different aptamer variants of the peptide SEQ ID NO: 4 FIG. 8: Representation of the homology model according to 4f5x.pdb (present in RCSB Protein Data Bank) (see also Table 1) Examples

Example 1 ; In vitro interaction study of EIN2 and ETR1

To detect the disruption of the interaction of EIN2 and ETR1, two different peptides were synthesized. The peptide, hereinafter referred to as NLSOP-1 (nuclear localization signal octapeptide), comprises an area which is suitable for interaction with ETR1. NLSOP-1 has the amino acid sequence SEQ ID NO: 4, which corresponds to the sequence H ₂ N-LKRYKRRL-COOH. The second peptide, which is referred to below as ROP-1 (random

octapeptide) contains a random sequence determined by ExPASy Random Protein Sequence Generator (http://web.expasy.org/randseq) and was used as a negative control. ROP-1 has the amino acid sequence SEQ ID NO: 97, which corresponds to the sequence H ₂ N-EFLYMSVN-COOH. The synthesis of both peptides was carried out by solid phase peptide synthesis using the device "Peptide Synthesizer 433A" from Applied Biosystems.

The effect of these two peptides on the EIN2-ETR1 interaction was examined by a quantitative method based on the fluorescence of the tryptophan with the purified recombinant proteins. Here are of a protein that participates in the interaction, all endogenous tryptophan residues removed. By adding this tryptophan-free protein to the interaction partner, its intrinsic fluorescence is quenched locally at the site of the interaction because the environment of the interaction partner changes here. This quenching can be used to determine the stability of the interaction and the

Determine dissociation constant of the complex.

This method as well as the method for producing the ETR1

Expression vector is described in Bisson MMA, A. Bleckmann, S. Allekotte, G. Groth, EIN2, the central regulator of ethylene signaling, is localized at the ER membrane where it interacts with the ethylene receptor ETR1, Brachem J: 424, 1-6; 2009, and MMA Bisson, G. Groth, New insight in ethylene signaling: autokinase activity of ETR1 modulates the interaction of receptors and EIN2, Molecular Plant: 5,882-889, 2010. Likewise, in the first mentioned publication, the method for the expression and purification of the full-length recombinant ETR1 (amino acid 1 -738) and E1N2 ^{479 "1294} EW, which is tryptop hanfrei and the carboxy-terminal portion of the protein has (amino acid 479-1294) Both recombinant proteins were isolated from Arabidopsis thaliana, cloned and expressed in Escherichia coli.

To a mixture of the protein ETR1 and either the peptide NLSOP-1 or ROP-1 in different concentrations was purified

Tryptophan-free EIN2 ^{479 ~ 1294} AW titrated step by step. The tryptophan fluorescence of the ETR1 was observed at 348 nm with an excitation wavelength of 295 nm. The resulting quenching of the fluorescence was against the

Concentration of the corresponding peptide applied and the

Dissociation constant calculated using the program GraFit (Erithacus Software Ltd.). A curve fit was used, which underpins the model that there is a single bond part per interaction partner. The dissociation constants given in FIG. 2 were characterized by three independent

Measurements are determined and the error bars show the standard deviation of these three measurements.

The dissociation constant of the complex EI 2 ^{ra "1Z94} EW with ETR1 as a function of the concentration of the peptides NLSOP-1 and ROP-1 is shown in Figure 2. It can be seen that ROP-1 has virtually no effect even at high concentrations of the peptide In contrast, there is a marked reduction in the affinity of ETR1 to EIN2 using NLSOP-1, inhibition of EIN2-ETR1 complex formation is proportional to the NLSOP-1 concentration, and the dissociation constants are quadrupled at 10 μΜ NSLOP-1 and increased thirty-fold at 200 μΜ NLSOP-1, suggesting a competitive displacement of EIN2 by NLSOP-1. These results indicate that interaction of a compound _" that can interact with the contact domain of ETR1 (NLSOP-1) inhibits the interaction of ETR1 with EIN2. Example 2: In planta interaction study of EIN2 and ETR1

For this purpose, the peptides which were described in detail in Example 1,

used. The interaction of a GFP-tagged EIN2 donor and a mCherry-tagged ETR1 (see Shaner, Nathan C, Campbell, Robert E. Steinbach, Paul A, Giepmans, Ben NG, Palmer, Amy E, Tsien, Roger Y (2004). "Improved monomeric red, orange and yellow fluorescent proteins derived from Disco- scoma sp. Red fluorescent protein." Nature Biotechnology 22 (12): 1587-72) as an acceptor was prepared by fluorescence resonance energy transfer (FREI) using confocal microscopy measured. The acceptor fluorophore was attached to the C-terminal end of the EIN2 and the donor to the C-terminal end of the ETR1. The transient

 Expression in Nicotiana benthamiana leaf epidermal cells was monitored as in MMA Bisson, A. Bleckmann, S. Allekotte, G. Groth, EIN2, the central regulator of ethylene signaling, is located at the ER membrane where it interacts with the ethylene receptor ETR1, Biochem J: 424, 1-8; 2009 and M, M.A. Bisson, G.Groth, New insight in ethylene signaling: autokinase activity of ETR1 modulates the

interaction of receptors and EIN2, Molecular Plant: 5,882-889, 2010. The leaves were incubated with 100 μL NLSOP-1 or 100 μM ROP-1 1 h before starting the measurement. A tandem construct of GFP and mCherry at EIN2

(ASEQ ID NO: 4) (i.e., an EIN2 not having SEQ ID NO: 4) was used as a positive control. The results show mean values

Standard deviations, where n = 15 cells.

The results of the FRET study are shown in FIG. The FRET efficiency between EIN2 and ETR1, which is obtained in the presence of ROP-1, is 12.0 ± 2.1%. It is thus similar to the value of the positive control (16.9%) and the value obtained in the absence of a peptide. Thus, ROP-1 has almost no effect on EIN2-ETR1 complex formation. In contrast, the energy transfer is reduced to 2.2 ± 1.0% when NLSOP-1 is used. This value is only slightly above the value of the background noise (1, 9%). These results show that interaction of a compound that can interact with the contact domain of ETR1 (NLSOP-1) also inhibits the interaction of ETR1 with EIN2 in planta.

Example 3: Inhibition of the Ethylene Response in Arabidopsis

To determine the ethylene response in living plants, the triple response of dark-grown Arabidopsis thaliana was investigated. In addition were

Wild type plants of Arabidopsis thaliana (Columbia ecotype) as described in M.M.A. Bisson, G.Groth, New insight in ethylene signaling: autokinase activity of ETR1 modulates the interaction of receptors and EIN2, Molecular Plant: 5,882-889, 2010. The peptides of Example 1 were added to the agar at various concentrations before the seeds were planted. The ethylene precursor used was 1-amino-cyano-propane-1-carboxylic acid (ACC). The

 Hypocotyl growth of the plants was determined as a characteristic feature of the triple response. For this purpose, the hypocotyl length of a plant, which in

Absence of ACC grew to 100% (negative control, first column from the left in Figure 4, labeled "Air") and all other measured lengths related to this length, and the results are taken as an average of 40 measurements

Standard deviation shown in Figure 4.

The maximum triple response was observed in plants grown in the presence of ACC, which was set as a positive control (second bar from the left in Figure 4, labeled "ACC"). The plants growing with increasing concentration of NSLOP-1 and ACC, showed an inhibited ethylene response (bars 3 to 8 from the left in Figure 4, with the concentration of NLSOP-1 indicated in each case.) The degree of inhibition correlates with the concentration of NLSOP-1 applied of a plant grown in the presence of 200 μM ROP-1 and ACC corresponds to the positive control (bar 9 from the left in Figure 4).

The results show that using the protein NLSOP-1 the

Triple response could be inhibited. Example 4: Inhibition of the Ethylene Response in Tomatoes

The influence of the NLSOP-1 peptide described in Example 1 on the inhibition of the ethylene response was investigated by the tomato maturation. For this, green, immature tomatoes were incubated with the peptide by two different treatment methods. The treated tomatoes and also untreated control tomatoes were stored in sample tubes sealed with aluminum foil for up to 20 days at room temperature in a windowless, dark room. The maturation process was documented at different times with a digital camera.

The following procedures were used to apply NLSOP-1 to the tomatoes:

Application 1: Surface treatment

A tomato was once coated with a 200 μΜ NLSOP-1 solution (dissolved in ultrapure water) using a brush.

Application 2: Incubation

A tomato was immersed for about 30 minutes in a 200 μΜ NLSOP-1 solution (dissolved in ultrapure water).

A total of two series of measurements were carried out. The visually determined

Results of a measurement series (color of the tomatoes) with the different ones

Different types of applications were averaged and these results can be summarized as follows (visual description of the color of the tomato, scale from green to yellow to red, where red represents a ripe tomato):

Table 5: Results of the visual description of the color of the treated tomatoes Incubation period control

 Application 1 Application 2

 in days after No NLSOP-NLSOP-1 NLSOP-1

 incubation 1

 0 green green green

 5 green, green, green to yellow

^■ yellow to

 10 green green

 light red

 15 green green red

 20 light yellow yellow red

These results show that the application of the peptide NLSOP-1 in any kind of application can delay the maturation of tomatoes. In particular, the external treatment of the tomato (application 1) is advantageous.

Example 5: In vitro interaction study of EIN2 and ETR1 - different peptides

In addition to Example 1, to demonstrate interference with the interaction of EIN2 and ETR1, additional peptides were synthesized which included a region suitable for interaction with ETR1.

The following table summarizes the data of the synthesized peptides: Table 8: Peptides used in Example 5

COOH

COOH

H ₂ N-

YSOP-2 LKRKFRRL-113 8 1116.8 -1.363 12.31

 COOH

H ₂ N-

YSOP-3 LKRKNRRL- 109 8 1084.4 -2.150 12.31

 COOH

H ₂ N-

YSOP-4 LKRLSRRL-100 8 1041, 7 -0,850 12,3

 COOH

H ₂ N-

YSOP-5 LKRKLRRL-112 8 1083.4 -1, 238 12.31

 COOH

H ₂ N-

YSOP-6 LKRKTRRL- 99 8 1070.7 -1, 800 12.31

 COOH

H ₂ N-

YSOP-7 LKRRKRRL-101 8 1126.1 -2.275 12.48

 COOH

H ₂ N-

AOP * -1 LDEYDEEL- 98 8 1025.5 -1, 400 3.39

 COOH

H ₂ N-

NLSOP ^{* 5} / NOP

 »1 LKRYKRRL-4 8 1131, 8 -1, 875 11, 73

 COOH

H ₂ N-

NLSOP / NOP-2 LKVYKRRL-111 8 1075.6 -0.787 11, 1

 COOH

H ₂ N-

NLSHP * ⁶ / NHP-KRYKRR-116 6 906.6 -3.767 11, 73 1

 COOH

 * R-K inversion octapeptides

* ² substitution-against-H-octapeptides

* ³ Y-substitution octapeptides

* ⁴ acidic octapeptides

* ⁵ nuclear localization signal octapeptides

* ⁶ nuclear localization signal hexapeptides

Synthesis of the peptides was performed by solid phase peptide synthesis (Fmoc strategy) and was purchased commercially from Thermo Scientific (Germany). ,

As in Voet van Vormizeele J & Groth G (2003) Heterologous expression and single-step purification of the EYRI from Arabidopsis thaliana. Protein Expr. Purtf. 32; 89-94 and Scharein B, Voet van Vormizeele J & Groth G (2008) Ethyiene signaiing: identifaction of a putative ETR1-AHP1 phosphorelay complex by fluorescence spectroscopy. Anal. Biochem. 377; 72-76 recombinant ETR1 (full-length) was isolated from Arabidopsis thaliana, cloned, heterologously expressed and isolated in Escherichia coli. Likewise, recombinant EIN2 ^{479 "1294} which has the carboxy-terminal portion of the protein (amino acid 479-1294) according to MMA bites, Bleckmann A, Allekotte S & Groth G (2009) EIN2, the central regulator of ethylene signaling, is localized at the ER ETR1, Biochem J. 424, 1-6 isolated from Arabidopsis thaliana, cloned, heterologously expressed and isolated in Escherichia coli The ETR1 protein was labeled with Alexa Fluor 488 as donor dye and the EIN2 ^{479 "1294} with Alexa Fluor 588 labeled as acceptor dye (both dyes are commercially available from Molecular Probes, Inc. and known to those skilled in the art). The

Protein labeling was carried out in a buffer system according to the manufacturer's instructions (50 mM potassium phosphate pH 8.0, 300 mM NaCl, 0.1% β-dodecyimaltoside, 0.002% RMSF).

Subsequently, the degree of fabling (DOL) was calculated photometrically. The labeled proteins were used for the following FRET test when a protein: dye ratio of 1: 1 was achieved. The labeled ETR1 and EIN2 ^{479 "1294} proteins became functional

Protein complex mixed. The protein complex solution was transformed into a white 384

Microtiter plate and fluorescence was determined using an Infinite M200pro microtiter plate reader (Tecan Deutschland GmbH, Craislheim, Germany). The donor fluorescence was excited at 455 nm and the acceptor emission was measured at a wavelength between 570 nm and 650 nm. The formation of the ETR1-EiN2 complex led to a Förster transfer between the donor and the acceptor dye. As a result, an increased acceptor emission could be observed.

In measuring the effect of the peptides of Table 5 shown above, the ETR1 -EIN2 protein complex was first probed with the respective compound

Final concentrations of 0.1 mM for 10 min at room temperature. The

Inhibition of ETR1-EIN2: Complex formation was determined by measuring the Acceptor fluorescence determined. The lower the emission, the less

Complex formation could be observed.

FIG. 5 shows the results of the measurement of the different compounds at a final concentration of 0.1 mM of the respective peptide (the percentage decrease in acceptor fluorescence is shown in comparison to a solution without addition of a peptide).

The results show that the compounds of SEQ ID NO: 109 to 1 16 inhibit the interaction of ETR1 with EIN2. In particular, it was possible to show that a hexapeptide according to the invention (SEQ ID NO: 116) also contains the abovementioned

Interaction inhibits. Furthermore, also show the different

octapeptides according to the invention that they are particularly suitable as a drug molecule to inhibit the complex formation between ETR1 and EIN2.

Example 6: In vitro interaction study of EIN2 and ETR1 sequence variants

To investigate the influence of a particular amino acid of the peptide of SEQ ID NO. 4 (NLSOP-1) on inhibition of ETR1-EIN2 complex formation, systematic alanine scanning mutagenesis was performed and each of the residues of the peptide of SEQ ID NO. 4, in each case exchanged for the amino acid alanine (see, for example, Morrison KL, Weiss GA (June 2001 j., "Combinatorial alanine scanning", Curr Opln Chem. Bio! 5 (3): 302-7, the method belongs to the knowledge of the expert.)

The following peptides were obtained:

Table 7: Alanine Scanning Mutagenesis Peptides

Name Sequence SEQ ID NO:

NLSOP-1 H ₂ N-LKRYKRRL-COOH 4

 AP1_L H2N-AKRYKRRL-COOH 117

AP2_K H ₂ N-LARYKRRL-COOH 118

AP3_R H ₂ N-LKAYKRRL-COOH 1 19 AP4_Y H ₂ N-LKRAKRRL-COOH 120

 AP5_K H2N-LKRYARRL-COOH 121

 AP6_R H2N-LKRYKARL-COOH 122

 AP7_R H2N-LKRYKRAL-COOH 123

 AP8 L H2N-LKRYKRRA-COOH 124

 ROP-1 H2N-EFLYMSVN-COOH 97

To analyze the inhibition of ETR1 -EIN2 complex formation, the FRET-based in vitro method described in Example 5 was used. The peptides were used in the assay at a concentration of 100 μΜ, since this corresponded to the IC50 value for the inhibition of ETR1 -EIN2 interaction by the starting peptide NLSOP-1 (SEQ ID NO: 4). The negative control used was the peptide ROP-1 (SEQ ID NO: 97).

The results are shown in Figure 6. All alanine substitution peptides show similar effects to the peptides of SEQ ID NO: 4. Therefore, it can be seen that the replacement of individual residues with alanine does not affect the overall effect of the peptide.

Example 7: In vitro interaction study of EIN2 and ETR1 aptamer variants Two aptamer variants of the peptide of SEQ ID NO: 4 were prepared and examined for their effect on the interaction of ERT1 and EIN2 using the FRET-based in vitro test system described in Example 5 , (Here, in measuring the effect of the aptamers, the ETR1 -EIN2 protein complex was first incubated with the respective compound at a final concentration of 0.03 mM for 10 min at room temperature). As a basis for the aptamer was thioredoxin A from E. coli with the sequence (MSDKIIHLTD DSFDTDVLKA DGAILVDFWA EWCGPCKMIA

PILDEIADEY QGKLTVAKLNIDQNPGTAPK YGIRGIPTLL LFKNGEVASA TKVGALSKGQ LKEFLDANLA; SEQ ID NO: 125). The aptamer sequences were inserted after the amino acid residue P35.

The following aptamers were prepared: Aptamer 1 (SEQ ID NO: 126)

 MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPPLLASVLKRYKRRLSENGPCKM IAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLKNGEVASATKVGALSK

GQLKEFLDANLA

Aptamer 2 (SEQ ID NO: 127):

 MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPPSVLKRYKRRLSNGFQFENGPC KMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLKNGEVASATKVGAL SKGQLKEFLDANLA

Both aptamer variants were heterologously expressed in E. coli and released from the

purified bacterial expression system. The negative control was thioredoxin A (Trx) without NLS sequence. First, the aptamers 1 and 2 and in the negative control Trx in a fixed concentration of 30 μΜ were used in the measurements. As can be seen from FIG. 6, in the presence of the aptamers there is a reduced energy transfer and thus a disruption of the ETR1-EIN2 interaction, whereas Trx without NLS sequence does not influence the interaction of ETR1 and EIN2.

 In measurements in which the concentration of Trx and the two aptamers was varied, it could be shown that the inhibition of the ETR1-EIN2 interaction by the two aptamers is concentration-dependent.

Example 8: Inhibition of the Ethylene Response in Tomatoes - Other Peptides The influence of the peptides described in Examples 5 and 6 on the inhibition of the ethylene response was investigated by the tomato maturation. For this purpose, as described in Example 4, green, immature tomatoes were incubated by the application method 1 with the peptide. A total of three series of measurements were carried out. The visually determined results of a series of measurements (color of the tomatoes) at the different times were averaged and these results can be summarized as follows (visual description of the color of the tomato, scale from green to yellow to red and dark red, where red represents a ripe tomato) : Table 8: Results of the visual description of the color of the treated tomatoes

Diese Ergebnisse zeigen, dass durch die Applikation der erfindungsgemäßen Peptide die Reifung der Tomaten verzögert werden kann. _

These results show that the application of the peptides according to the invention can delay the maturation of tomatoes. _

Claims

claims A composition for influencing the maturation process, the senescence process and / or the stress control of plants and / or their fruits comprising at least one compound which is selected from the group consisting of a peptide, a peptide mimetic, an antibody and / or its fragments and an aptamer, characterized in that the peptide or antibody and / or fragments thereof comprises an amino acid sequence selected from the group consisting of  Amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3 that the peptide mimetic modified at least one backbone on the peptide Amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, or that the aptamer is prepared on the basis of the target structure of a peptide, wherein the peptide is selected from the amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the Amino acid sequence SEQ ID NO: 3, a permutation of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which at least 4, preferably at least 5, more preferably at least 6 of the in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of the Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, wherein compounds are excluded, wherein the peptide or antibody and / or fragments thereof has an amino acid sequence of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100 , SEQ ID NO: 101 or SEQ ID NO: 102, and / or a part of one of the amino acid sequences SEQ ID NO: 98 to SEQ ID NO: 102, which is at least 6 of those mentioned in SEQ ID NO: 98 to SEQ ID NO: 102 And / or comprises a derivative of the amino acid sequences SEQ ID NO: 98 to 102 and / or in which a peptide mimetic consists of a peptide backbone-modified amino acid sequence which is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO : 99, SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 02, and / or wherein an aptamer is prepared based on the target structure of a peptide, wherein the peptide is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100 SEQ ID NO: 101 and SEQ ID NO: 102. 2. comprising agents for influencing the maturation process, the senescence process and / or the stress tolerance of plants and / or their fruits at least one compound which is selected from the group consisting of a peptide, a peptide mimetic, an aptamer, an antibody and / or its fragments, characterized in that the peptide or antibody and / or its fragments have the amino acid sequence SEQ ID NO: 103, a part of the amino acid sequence SEQ ID NO: 103, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 103, or a derivative of the Amino acid sequence SEQ ID NO: 103 comprises that the peptide mimetic modified the peptide backbone modified amino acid sequence SEQ ID NO: 103, a part of a peptide backbone Amino acid sequence SEQ ID NO: 103, which at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 103 comprises, or a derivative of a peptide backbone modified amino acid sequence SEQ ID NO: 103 comprises or that the aptamer is prepared based on the target structure of a peptide, wherein the peptide is selected from the amino acid sequence SEQ ID NO: 103, a part of one of the amino acid sequences SEQ ID NO: 103, which is at least 4, preferably at least 5, particularly preferably at least 6 of those mentioned in SEQ ID NO: 103 Amino acid, and a derivative of the amino acid sequence SEQ ID NO: 103, wherein when the amino acid sequence SEQ ID NO: 103 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 103 alanine. 3. Composition according to claim 1 or 2, characterized in that the agent is the interaction of the protein EIN2 (Ethylene Insensitive 2) or an orthologous protein thereof with the receptor protein ETR1 (Ethylene resistant 1), its isoforms ERS1, ETR2, ERS2 , EIN4 or homologous or orthologous Proteins thereof by interaction with a contact domain of the ethylene receptor ETR1 or its isoforms ERS1, ETR2, ERS2, EIN4 or a homologous or orthologous protein thereof. 4. Composition according to one of claims 1 to 3, characterized in that the means comprises at least one further compound which is adapted to influence the maturation process, the senescence process and / or the stress tolerance of plants and / or their fruits. 5. Composition according to claim 4, characterized in that the at least one further compound is an ethylene antagonist. 6. A compound which is selected from the group consisting of a peptide, a peptide mimetic and an aptamer, characterized in that the peptide consists of an amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 1, of the Amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a Part of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3 that the Peptide mimetic consists of a modified on the peptide backbone amino acid sequence, which is selected from the group consisting of Amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3 or that the aptamer is prepared on the basis of the target structure of a peptide, wherein the peptide is selected from the amino acid sequence SEQ ID NO: 1, the amino acid sequence  SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, wherein compounds are excluded in which the peptide from a Amino acid sequence of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 or SEQ ID NO: 102, and / or a part of one of Amino acid sequences SEQ ID NO: 98 to SEQ ID NO: 102, which comprises at least 6 of the amino acids mentioned in SEQ ID NO: 98 to SEQ ID NO: 102 and / or consists of a derivative of the amino acid sequences SEQ ID NO: 98 to 102 and / or wherein a peptide mimetic consists of a peptide backbone-modified amino acid sequence selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 02, and / or wherein an aptamer is prepared based on the target structure of a peptide, wherein the peptide is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100 SEQ ID NO: 101 and SEQ ID NO: 102. 7. A compound which is selected from the group consisting of a peptide, a peptide mimetic an antibody and / or its fragments and an aptamer, characterized in that the peptide and / or the antibody and / or its fragments, the amino acid sequence SEQ ID NO : 103, or a part of the amino acid sequence SEQ ID NO: 103, which comprises at least 4, preferably at least 5, particularly preferably at least 6 of the amino acids mentioned in SEQ ID NO: 103, or comprises a derivative of the amino acid sequence SEQ ID NO: 103 or the peptide mimetic modified at the peptide backbone Amino acid sequence SEQ ID NO: 103 or a part of the amino acid sequence modified on the peptide backbone SEQ ID NO: 103 which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 103, or a derivative of the peptide backbone modified  Amino acid sequence SEQ ID NO: 103 or that the aptamer is prepared on the basis of the target structure of a peptide, wherein the peptide is selected from the amino acid sequence SEQ ID NO: 103, a part of the amino acid sequence SEQ ID NO: 103, which at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 03, and a derivative of the amino acid sequence SEQ ID NO: 103, wherein, when the Amino acid sequence SEQ ID NO: 103 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 103 is alanine. 8. A compound according to claim 7, characterized in that the peptide, the antibody and / or its fragments at least one An amino acid sequence selected from the group consisting of SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 110, SEQ ID NO: 111, SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO : 114, SEQ ID NO: 115, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 118, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122 , SEQ ID NO: 123 and SEQ ID NO: 124, a permutation of one of Amino acid sequences SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 110, SEQ ID NO: 111, SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO: 114, SEQ ID NO: 115, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 118, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO : 124, a part of one of the amino acid sequences SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 1 10, SEQ ID NO: 11, SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO: 114, SEQ ID NO: 11, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 118, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, which comprises at least 4, preferably at least 5, particularly preferably at least 6 of the amino acids mentioned in SEQ ID NO: 4, SEQ ID NO: 109 to SEQ ID NO: 124, and a derivative of any of the amino acid sequences of SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 110, SEQ ID NO: 11 1, SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO: 114, SEQ ID NO: 1 15, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 1 18, SEQ ID NO: 1 19, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, or the peptide mimetic a peptoid or the like r represents D-peptide having a biological activity similar to an amino acid sequence selected from the group consisting of SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 110, SEQ ID NO: 11 1, SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO: 114, SEQ ID NO: 115, SEQ ID NO: 116, SEQ ID NO: 11, SEQ ID NO: 118, SEQ ID NO: 1 19, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, a permutation of one of the amino acid sequences SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO : 1 10, SEQ ID NO: 11 1, SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO: 114, SEQ ID NO: 1 15, SEQ ID NO: 116, SEQ ID NO: 1,17, SEQ ID NO: 118, SEQ ID NO: 1 19, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, a part of one of the amino acid sequences SEQ ID NO : 4, SEQ ID NO: 109, SEQ ID NO: 110, SEQ ID NO: 111, SEQ ID NO: 1 12, SEQ ID NO: 1 13, SEQ ID NO: 114, SEQ ID NO: 115, SEQ ID NO : 116, SEQ ID NO: 11, SEQ ID NO: 118, SEQ ID NO: 1 19, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 24, which at least 4, preferably at least 5, particularly preferably at least 6 of the in SEQ ID NO: 4, SEQ ID NO: 109 to SEQ ID NO: 124, and a derivative of one of the amino acid sequences SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 110, SEQ ID NO: 11, SEQ ID NO: 112, SEQ ID NO: 13, SEQ ID NO: 114, SEQ ID NO: 1 15, SEQ ID NO: 16, SEQ ID NO: 117, SEQ ID NO: 1 18, SEQ ID NO: 1 19, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, or the aptamer Based on the target structure of a peptide, wherein the peptide is selected from the group consisting of SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 1 10, SEQ ID NO: 11 1, SEQ ID NO: 1 12, SEQ ID NO: 113, SEQ ID NO: 114, SEQ ID NO: 115, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 118, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, a permutation of one of the amirous acid sequences SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 110, SEQ ID NO : 11, SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO: 14, SEQ ID NO: 115, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 1 18, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, a part of one of the amirosacetic acid sequences SEQ ID NO: 4, SEQ ID NO: 109 , SEQ ID NO: 1 10, SEQ ID NO: 11, SEQ ID NO: 1 12, SEQ ID NO: 113, SEQ ID NO: 14, SEQ ID NO: 1 15, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 1 18, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO : 121, -SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124, which at least 4, preferably at least 5, more preferably at least 6 of the in SEQ ID NO: 4, SEQ ID NO: 109 to SEQ ID NO: 124, and a derivative of one of Amino acid sequences SEQ ID NO: 4, SEQ ID NO: 109, SEQ ID NO: 1 10, SEQ ID NO: 111, SEQ ID NO: 1 12, SEQ ID NO: 1 13, SEQ ID NO: 1 14, SEQ ID NO : 1-15, SEQ ID NO: 16, SEQ ID NO: 117, SEQ ID NO: 118, SEQ ID NO: 1 19, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123 and SEQ ID NO: 124. 9. Process for influencing the maturation process, the  Seneszenzprozesses and / or the stress tolerance of plants and / or their fruits, characterized in that in the plants and / or fruits the Interaction of the protein EIN2 (Ethylene Insensitive 2) or an orthologous protein thereof with the receptor protein ETR1 (Ethylene resistant 1), its isoforms ERS1, ETR2, ERS2, EIN4 or homologous or orthologous proteins thereof by the Interaction of a compound selected from the group consisting of a peptide, a peptide mimetic, an aptamer, an antibody and / or its fragments and mixtures of these compounds with a contact domain of the invention Ethylene receptor ETR1 or its isoforms ERS1, ETR2, ERS2, EIN4 or a homologous or orthologous protein thereof is inhibited, wherein the contact domain is the one with EIN2 or an orthologous Protein thereof interacts, and wherein the peptide, the antibody and / or its fragments at least one Amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of  Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, the peptide mimetic at least one modified at the peptide backbone Amino acid sequence which is selected from the group consisting of the amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of  Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, or the aptamer is prepared based on the target structure of a peptide, wherein the peptide is selected from the amino acid sequence SEQ ID NO: 1, the amino acid sequence SEQ ID NO: 2, the amino acid sequence SEQ ID NO: 3, a permutation of one of the amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, a part of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 1 to SEQ ID NO: 3, and a derivative of one of Amino acid sequences SEQ ID NO: 1 to SEQ ID NO: 3, excluding compounds in which the peptide or antibody and / or fragments thereof have an amino acid sequence of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 or SEQ ID NO: 102, and / or a part of one of the amino acid sequences SEQ ID NO: 98 to SEQ ID NO: 102, which contains at least 8 of SEQ ID NO 98 to SEQ ID NO: 102 comprises and / or comprises a derivative of the amirous acid sequences SEQ ID NO: 98 to 102 and / or in which a peptide mimetic consists of a peptide backbone modified amino acid sequence which is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101 and SEQ ID NO: 102, and / or wherein an aptamer is prepared based on the target structure of a peptide, wherein the peptide is selected is selected from the group consisting of SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100 SEQ ID NO: 101 and SEQ ID NO: 102. 10. Method for influencing the maturation process, the Senescence process and / or the stress tolerance of plants and / or their Fruits, characterized in that in the plants and / or fruits the Interaction of the protein EIN2 (Ethylene Insensitive 2) or an orthoiogenic protein thereof with the receptor protein ETR1 (Ethylene resistant 1), its isoforms ERS1, ETR2, ERS2, EIN4 or homologous or orthoiogenic proteins thereof by the interaction of a compound selected from A group consisting of a peptide, a peptide mimetic, an aptamer, an antibody and / or its fragments, small molecules and mixtures of these compounds with a contact domain of the ethylene receptor ETR1 or its isoforms ERS1, ETR2, ERS2, EIN4 or a homologous or orthoiogenic protein thereof wherein the contact domain is that which interacts with EIN2 or an orthoiogenic protein thereof and wherein the peptide, the antibody and / or its fragments at least one Amino acid sequence SEQ ID NO: 103, a part of the amino acid sequence SEQ ID NO: 103 which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 03, or a derivative of the amino acid sequence SEQ ID NO: 103 includes, the peptide mimetic has at least one backbone modified on the peptide Amino acid sequence SEQ ID NO: 103, a part of the peptide backbone modified amino acid sequence SEQ ID NO: 103, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 103, or a derivative modified on the peptide backbone Amino acid sequence SEQ ID NO: 103 or the aptamer is prepared on the basis of the Zieistruktur of a peptide, wherein the peptide is selected from the amino acid sequence SEQ ID NO: 103, a part of Amino acid sequence SEQ ID NO: 103, which comprises at least 4, preferably at least 5, particularly preferably at least 6, of the amino acids mentioned in SEQ ID NO: 103, and a derivative of the amino acid sequence SEQ ID NO: 103, where if the amino acid sequence SEQ ID NO: 103 at one position comprises alanine, none of the other amino acids of SEQ ID NO: 103 is alanine. 11. The method according to any one of claims 9 or 10, characterized in that the compound which is selected from the group consisting of a peptide, a peptide mimetic, an aptamer, an antibody and / or its fragments and mixtures of these compounds, a water solubility of at pH = 7 and 20 ° C of at least 1 g / L. 12. The method according to claim 9, characterized in that the peptide consists of an amino acid sequence which is selected from the group, consisting of the amino acid sequence SEQ ID NO: 3, a permutation of Amino acid sequence SEQ ID NO: 3, a part of the amino acid sequence SEQ ID NO: 3, which comprises at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 3, and a derivative of Amino acid sequences SEQ ID NO: 3 or that the peptide mimetic consists of an amino acid sequence modified on the peptide backbone, which is selected from the group consisting of the amino acid sequence SEQ ID NO: 3, a permutation of the amino acid sequence SEQ ID NO: 3, a part of the amino acid sequence SEQ ID NO: 3, which is at least 4, preferably at least 5, more preferably at least 6 of the amino acids mentioned in SEQ ID NO: 3, and a derivative of the amino acid sequences SEQ ID NO: 3. 13. The method according to any one of claims 10 to 12, characterized in that the orthologous protein of the EIN2 an amino acid sequence which is selected from the group consisting of SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 41, SEQ ID NO: 42, SEQ ID NO: 43, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46, SEQ ID NO: 47, SEQ ID NO: 48, SEQ ID NO: 49, SEQ ID NO: 50, SEQ ID NO: 51, SEQ ID NO: 52 and SEQ ID NO: 53. 14. The method according to any one of claims 10 to 13, characterized in that the orthologous protein of the ETR1 or its isoforms an amino acid sequence which is selected from the group consisting of SEQ ID NO: 54,  SEQ ID NO: 55, SEQ ID NO: 56, SEQ ID NO: 57, SEQ ID NO: 58, SEQ ID NO: 59, SEQ ID NO: 60, SEQ ID NO: 61, SEQ ID NO: 62, SEQ ID NO: 63, SEQ ID NO: 64, SEQ ID NO: 65, SEQ ID NO: 66, SEQ ID NO: 67, SEQ ID NO: 68, SEQ ID NO: 69, SEQ ID NO: 70, SEQ ID NO: 71, SEQ ID NO: 72, SEQ ID NO: 73, SEQ ID NO: 74, SEQ ID NO: 75, SEQ ID NO: 76, SEQ ID NO: 77, SEQ ID NO: 78, SEQ ID NO: 79, SEQ ID NO: 80, SEQ ID NO: 81, SEQ ID NO: 82, SEQ ID NO: 83, SEQ ID NO: 84, SEQ ID NO: 85, SEQ ID NO: 86, SEQ ID NO: 87, SEQ ID NO: 88, SEQ ID NO: 89, SEQ ID NO: 90, SEQ ID NO: 91, SEQ ID NO: 92, SEQ ID NO: 93, SEQ ID NO: 94, SEQ ID NO: 95 and SEQ ID NO: 96 or that the homologous protein of ETR1 has an amino acid sequence which is selected from the group consisting of SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9 , SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, S EQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28 SEQ ID NO : 29 and SEQ ID NO: 30. 15. The method according to any one of claims 10 to 14, characterized in that the plants are selected from the group consisting of useful plants and ornamental plants and their fruits are selected from the group consisting of the fruits of crops and ornamental plants.