DE19822406A1 - Composition for treating cancer and other diseases caused by pathogenic proteins - Google Patents
Composition for treating cancer and other diseases caused by pathogenic proteinsInfo
- Publication number
- DE19822406A1 DE19822406A1 DE1998122406 DE19822406A DE19822406A1 DE 19822406 A1 DE19822406 A1 DE 19822406A1 DE 1998122406 DE1998122406 DE 1998122406 DE 19822406 A DE19822406 A DE 19822406A DE 19822406 A1 DE19822406 A1 DE 19822406A1
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- proteins
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- immunogenic
- mip
- protease
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Links
- 102000004169 proteins and genes Human genes 0.000 title claims description 21
- 108090000623 proteins and genes Proteins 0.000 title claims description 21
- 206010028980 Neoplasm Diseases 0.000 title claims description 7
- 201000011510 cancer Diseases 0.000 title claims description 5
- 201000010099 disease Diseases 0.000 title description 5
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 title description 5
- 230000001717 pathogenic effect Effects 0.000 title 1
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 27
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 14
- 108090000317 Chymotrypsin Proteins 0.000 claims abstract description 12
- 229960002376 chymotrypsin Drugs 0.000 claims abstract description 12
- 108091005804 Peptidases Proteins 0.000 claims abstract description 8
- 239000004365 Protease Substances 0.000 claims abstract description 8
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract description 8
- 230000001225 therapeutic effect Effects 0.000 claims abstract description 4
- 230000002163 immunogen Effects 0.000 claims description 23
- 238000002360 preparation method Methods 0.000 claims description 16
- 230000003993 interaction Effects 0.000 claims description 6
- 102000009091 Amyloidogenic Proteins Human genes 0.000 claims description 5
- 108010048112 Amyloidogenic Proteins Proteins 0.000 claims description 5
- 102000029797 Prion Human genes 0.000 claims description 4
- 108091000054 Prion Proteins 0.000 claims description 4
- 102000027450 oncoproteins Human genes 0.000 claims description 4
- 108091008819 oncoproteins Proteins 0.000 claims description 4
- 238000010353 genetic engineering Methods 0.000 claims description 2
- 230000028993 immune response Effects 0.000 claims 1
- 239000000427 antigen Substances 0.000 abstract description 12
- 102000036639 antigens Human genes 0.000 abstract description 12
- 108091007433 antigens Proteins 0.000 abstract description 12
- 229920001184 polypeptide Polymers 0.000 abstract 1
- 238000003786 synthesis reaction Methods 0.000 description 7
- 230000000694 effects Effects 0.000 description 5
- 108010038061 Chymotrypsinogen Proteins 0.000 description 4
- 101710180319 Protease 1 Proteins 0.000 description 4
- 101710137710 Thioesterase 1/protease 1/lysophospholipase L1 Proteins 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- -1 B. immune complexes Proteins 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 229940088598 enzyme Drugs 0.000 description 3
- CFYIUBWVKZQDOG-UHFFFAOYSA-N 4-[[2-[[2-[[1-(4-nitroanilino)-1-oxo-3-phenylpropan-2-yl]amino]-2-oxoethyl]amino]-2-oxoethyl]amino]-4-oxobutanoic acid Chemical compound C=1C=C([N+]([O-])=O)C=CC=1NC(=O)C(NC(=O)CNC(=O)CNC(=O)CCC(=O)O)CC1=CC=CC=C1 CFYIUBWVKZQDOG-UHFFFAOYSA-N 0.000 description 2
- 208000024781 Immune Complex disease Diseases 0.000 description 2
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 2
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 2
- 230000000536 complexating effect Effects 0.000 description 2
- 230000006641 stabilisation Effects 0.000 description 2
- 238000011105 stabilization Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 101710132601 Capsid protein Proteins 0.000 description 1
- 101710094648 Coat protein Proteins 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 206010018364 Glomerulonephritis Diseases 0.000 description 1
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 101710125418 Major capsid protein Proteins 0.000 description 1
- 102000007474 Multiprotein Complexes Human genes 0.000 description 1
- 108010085220 Multiprotein Complexes Proteins 0.000 description 1
- 101710141454 Nucleoprotein Proteins 0.000 description 1
- 101710083689 Probable capsid protein Proteins 0.000 description 1
- 208000007536 Thrombosis Diseases 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 206010047115 Vasculitis Diseases 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 206010003246 arthritis Diseases 0.000 description 1
- 230000001588 bifunctional effect Effects 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 238000000034 method Methods 0.000 description 1
- 231100000219 mutagenic Toxicity 0.000 description 1
- 230000003505 mutagenic effect Effects 0.000 description 1
- 201000008383 nephritis Diseases 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 229910052713 technetium Inorganic materials 0.000 description 1
- GKLVYJBZJHMRIY-UHFFFAOYSA-N technetium atom Chemical compound [Tc] GKLVYJBZJHMRIY-UHFFFAOYSA-N 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
- A61K38/46—Hydrolases (3)
- A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
- A61K38/482—Serine endopeptidases (3.4.21)
- A61K38/4826—Trypsin (3.4.21.4) Chymotrypsin (3.4.21.1)
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Chemical & Material Sciences (AREA)
- Epidemiology (AREA)
- Animal Behavior & Ethology (AREA)
- General Health & Medical Sciences (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Abstract
Description
Die Erfindung betrifft den Bereich Proteinengineering, Enzymologie und Immunologie, und kann als ein therapeutisches Präparat gegen Krebs und viele andere Erkrankungen verwendet werden, die durch verschiedenen Proteine oder Proteinkomplexe wie z. B. Immunkomplexe, Oncoproteine, Prionen, Distrophine, Amyloidproteine u.v.a., verursacht werden.The invention relates to the field of protein engineering, enzymology and immunology, and can can be used as a therapeutic preparation against cancer and many other diseases through different proteins or protein complexes such as B. immune complexes, oncoproteins, Prions, distrophins, amyloid proteins and many more.
In der heutigen Zeit gibt es keine wirksame Präparate gegen Immunkomplexkrankheiten, d. h. Präparate, die Immunkomplexe spalten und lösen können, ohne anderen Proteinen, Zellen und Geweben des Körpers zu schädigen.At the present time, there are no effective preparations against immune complex diseases, i. H. Preparations that can split and dissolve immune complexes without other proteins, cells and Damaging tissues of the body.
Es gibt auch keine wirksame Präparate gegen Krankheiten, die durch Prionen, Distrophine, Amyloidproteinen u. a. gefährlichen Proteinen verursacht werden.There are also no effective preparations against diseases caused by prions, distrophins, Amyloid proteins and the like a. dangerous proteins.
Mehrere Präparate wirken auf Enzyme, d. h. entweder beschleunigen oder hemmen ihre Aktivität.Several preparations act on enzymes, i.e. H. either accelerate or inhibit their activity.
Die Zahl der Nebenwirkungen eines Präparats ist von seiner chemischen Struktur abhängig. Ein nicht-proteinartiges, chemisch einfach aufgebautes Molekül kann auch unerwünscht nicht nur auf ein bestimmtes Enzym wirken, sondern auch auf anderen Enzyme, Zellen und Geweben, und damit stört solch ein Präparat den Stoffwechsel im Organismus.The number of side effects of a preparation depends on its chemical structure. A Non-proteinaceous, chemically simple molecules can not only be undesirable a particular enzyme act, but also on other enzymes, cells and tissues, and thus such a preparation disrupts the metabolism in the organism.
Es gibt eine Forschung, die "Synthese und Konformationsstabilisierung Antigenbindender Peptide" heisst, und befasst sich mit der chemischen Synthese und Konformationsstabilisierung von Peptiden, die Sequenzabschnitte der hypervariablen Regionen der Immunglobuline enthalten. Diese Moleküle werden auf ihre Fähigkeit untersucht, ein bestimmtes Antigen zu binden. (s. Forschungsbericht 1993 des Insitutes der Molekularen Immunologie in Berlin).There is a research called "Synthesis and Conformational Stabilization of Antigen Binding Peptides" means, and deals with the chemical synthesis and conformational stabilization of Peptides containing sequence sections of the hypervariable regions of the immunoglobulins. This Molecules are examined for their ability to bind a specific antigen. (see Research report 1993 from the Institute of Molecular Immunology in Berlin).
Es gibt eine andere Forschung, die "Tc-komplexierende Peptide" heisst, und befasst sich mit der Modellierung und gentechnischen bzw. peptidchemischen Konstruktion von tumorgerichteten, antikörperanalogen Proteinen mit gleichzeitig Technetium-komplexierenden Eigenschaften.There is another research called "Tc Complexing Peptides" which is concerned with Modeling and genetic engineering or peptide chemical construction of tumor-directed, antibody-analogous proteins with technetium complexing properties.
Diese bifunktionalen Moleküle dienen zum immunoscintigraphischen Einsatz in der Tumordiagnostik. (s. Forschungsbericht 1993 des Institutes der Molekularen Immunologie in Berlin).These bifunctional molecules are used for immunoscintigraphic purposes Tumor diagnosis. (see research report 1993 by the Institute of Molecular Immunology in Berlin).
Es gibt noch eine Forschung, die "Protein-Engineering nach dem Baukastenprinzip mittels chemischer Synthese am Beispiel von Antikörperfragmenten" heisst, und hat das Ziel, die chemische Synthese von Antikörperfragmenten und anderen neuartigen Antiken bindenden Peptiden und Peptid-Mimetika mit gegenüber kompletten Antikörpern vergleichbaren Antigen- Bindungseigenschaften. Weiterhin ist die Synthese einer Peptid-Epitop-Bibliothek zur Charakterisierung der Bindungsspezifitäten dieser Mini-Antikörper geplant. Diese Moleküle werden mit Hilfe der schrittweisen Synthese, aber auch durch Fragmentkondensationstechniken hergestellt. Sie werden auf ihre Fähigkeit untersucht, ein bestimmtes Antigen spezifisch zu binden. (s. Forschungsbericht 1993 des Institutes der Molekularen Immunologie).There is still research that uses "modular protein engineering chemical synthesis using the example of antibody fragments "means and has the goal of chemical synthesis of antibody fragments and other novel antigen binding Peptides and peptide mimetics with antigen comparable to complete antibodies Binding properties. Furthermore, the synthesis of a peptide-epitope library is available Characterization of the binding specificities of these mini antibodies is planned. These molecules with the help of step-by-step synthesis, but also through fragment condensation techniques manufactured. They are examined for their ability to specifically bind a specific antigen. (see research report 1993 by the Institute of Molecular Immunology).
Die Aufgabe der Erfindung ist die Schaffung eines starken Präparats gegen Krebs und Krankheiten, die durch gefährlichen Proteinen verursacht werden. Das Präparat soll selektiv auf diese Proteinen reagieren und spalten, so dass sie im Organismus gelöst werden können. Dabei soll dieses Präparat auch wenig Nebenwirkungen haben. The object of the invention is to create a strong preparation against cancer and Diseases caused by dangerous proteins. The preparation should be selective these proteins react and cleave so that they can be dissolved in the organism. In doing so this preparation also have few side effects.
Die bekanntesten Krankheiten, die durch solchen Proteine verursacht werden, sind z. B. Nephritis (Glomerulonephritis u. a. Arten), Arthritis, Uvetitis, Vasculitis und v.a. (Immunkomplexkrankheiten, s. "Immunology, Immunopathology und Immunity" St. Sell, fourth edition, s. 378-395), Alzheimer (Amyloidproteinen, s. "Neuroscience" D. Purves, B. Augustine, D. Fitzpatrick u. a., s. 560-561). Distrophie (Distrophinproteinen), Krebs (teilweise Oncoproteinen, s. "Molecular Cell Biology" H. Lodish, D. Baltimore, A. Berk u. a., third edition, Kap.: Cancer), Jakob-Crutzfeldt- Krankheit, Mad-Cow-Krankheit u. a. (Prionproteinen, s. Concise Encyclopedia of Biochemistry and Molecular Biology, s. Prion).The best known diseases caused by such proteins are e.g. B. nephritis (Glomerulonephritis and other species), arthritis, uvetitis, vasculitis and especially (Immune complex diseases, s. "Immunology, Immunopathology and Immunity" St. Sell, fourth edition, p. 378-395), Alzheimer's (amyloid proteins, see "Neuroscience" D. Purves, B. Augustine, D. Fitzpatrick et al., See 560-561). Distrophy (distrophin proteins), cancer (partially oncoproteins, see "Molecular Cell Biology "H. Lodish, D. Baltimore, A. Berk et al., Third edition, chap .: Cancer), Jakob-Crutzfeldt- Illness, Mad Cow Disease & a. (Prion proteins, see Concise Encyclopedia of Biochemistry and Molecular Biology, s. Prion).
Die Aufgabe der Erfindung wird dadurch gelöst, dass eine Protease, z. B. Chymotrypsin durch eine genmanipulative Weise mit einem oder mehreren immunogenischen Peptiden gekoppelt wird; dadurch entsteht der Proteinkomplex MIP/MIC (Monoklonale Immunogenische Protease) Monoklonales Immunogenisches Chymotrypsin), der die Immunreaktion des Organismus auf Immunkomplexe, Prionen, Amyloidproteine u. a. gefährlichen Proteine verbessert. Bei der Interaktion vom immunogenischen Peptid des MIP/MIC mit einem der obenerwähnten Proteinen, wird dieses durch die Protease des MIP/MIC in der Ort der Interaktion gespaltet. Folglich können diese Proteine durch mehreren MIP/MIC gespaltet, und im Organismus gelöst werden.The object of the invention is achieved in that a protease, for. B. chymotrypsin by a is genetically manipulated with one or more immunogenic peptides; this creates the protein complex MIP / MIC (Monoclonal Immunogenic Protease) Monoclonal immunogenic chymotrypsin), which controls the immune response of the organism Immune complexes, prions, amyloid proteins and the like. a. dangerous proteins improved. In the Interaction of the MIP / MIC immunogenic peptide with one of the above Proteins, this is cleaved by the protease of the MIP / MIC in the place of the interaction. Hence these proteins can be cleaved by several MIP / MIC and dissolved in the organism.
Die Ansätze auf innere Wände der Gefässen, und Thrombosen können dadurch auch gelöst werden.The approaches to inner walls of the vessels, and thromboses can also be resolved become.
Für die Synthese des MIP/MIC wird die DNA einer Protease, z. B. Chymotrypsin durch Ligase mit der DNA eines immunogenischen Peptids verbunden. Die dadurch entstandene DNA wird in das E. coli Expressionssystem oder in eukaryotisches Expressionssystem implantiert.For the synthesis of the MIP / MIC, the DNA of a protease, e.g. B. Chymotrypsin by ligase linked to the DNA of an immunogenic peptide. The resulting DNA is in the E. coli expression system or implanted in eukaryotic expression system.
Es sollen im Produkt MIC folgende Unterschiede vom Chymotrypsin vorhanden sein: The following differences from chymotrypsin should exist in the product MIC:
1). A. Chain (13 aa) wird auf einen bestimmten Abschnitt vor dem C-terminus, d. h. -COOH verlängert, weil ein bestimmtes immunogenisches Peptid in diesem Abschnitt entsteht.1). A. Chain (13 aa) is placed on a certain section in front of the C-terminus, i.e. H. -COOH extended because a certain immunogenic peptide is formed in this section.
2). C. Chain (97 aa) wird auf einen bestimmten Abschnitt vor dem C-terminus verlängert, weil ein bestimmtes immunogenisches Peptid in diesem Abschnitt entsteht.2). C. Chain (97 aa) is extended to a certain section before the C-terminus because a specific immunogenic peptide is created in this section.
Das Chymotrypsinogen (Fig. 3 und 6) soll folglich verändert werden:The chymotrypsinogen ( Fig. 3 and 6) should therefore be changed:
1). Der Abschnitt eines bestimmten immunogenischen Peptids wird z. B. zwischen 12 aa und 13 aa gelagert.1). The section of a particular immunogenic peptide is e.g. B. between 12 aa and 13 aa stored.
2). Der Abschnitt eines bestimmten immunogenischen Peptids wird z. B. zwischen 220 aa oder 244 aa und 245 aa gelagert.2). The section of a particular immunogenic peptide is e.g. B. between 220 aa or 244 aa and 245 aa stored.
Die DNA des Chymotrypsinogens soll entsprechend verändert werden.The DNA of the chymotrypsinogen should be changed accordingly.
Die immunogenischen Peptiden des MIC sollen ein bestimmtes Antigen im Organismus finden, das vom Chymotrypsin des MIC gespaltet, und im Organismus gelöst wird.The immunogenic peptides of the MIC are supposed to find a specific antigen in the organism, which is split by the chymotrypsin of the MIC and is dissolved in the organism.
Das Antigen, das auf solche Weise vernichtet werden soll, kann ein Immunkomplex, ein Distrophin, ein Prion, ein Oncoprotein, ein Hüllprotein eines Viruses, ein Amyloidprotein usw. sein.The antigen to be destroyed in this way can be an immune complex Distrophin, a prion, an oncoprotein, a coat protein of a virus, an amyloid protein, etc.
Auf anderen Körperproteinen, Zellen und Geweben soll MIC nicht reagieren. Deswegen soll das Präparat wenig Nebenwirkungen haben.MIC should not react to other body proteins, cells and tissues. That's why Preparation have few side effects.
Bei der Verwendung dieses Präparats wird folgendes Ergebnis erreicht:When using this preparation the following result is achieved:
1). Selektive Vernichtung der gefährlichen mutagenischen Proteinen. Die normale Körperproteinen Zellen und Geweben bleiben dabei verschont.1). Selective destruction of the dangerous mutagenic proteins. The normal one Body proteins cells and tissues are spared.
2). Weniger Nebenwirkungen als bisherige Präparate. 2). Less side effects than previous preparations.
In der Fig. 1 ist schematisch eine monoklonale immunogenische Protease dargestellt. Sie besteht aus einer Protease 1 und immunogenischen Zonen 2.A monoclonal immunogenic protease is shown schematically in FIG . It consists of a protease 1 and immunogenic zones 2 .
In der Fig. 2 ist schematisch eine monoklonale immunogenische Protease dargestellt, die aber nicht nur die Protease 1 und immunogenischen Zonen 2 enthält, sondern auch die monoklonale immunogenischen Peptiden 3.In FIG. 2, a monoclonal immunogenic protease is shown schematically, but which contains not only the Protease 1 and immunogenic zones 2, but also the monoclonal immunogenic peptides. 3
In der Fig. 3 sind Chymotrypsinogen und a-chymotrypsin dargestellt.In FIG. 3, chymotrypsinogen and a-chymotrypsin shown.
In der Fig. 4 ist das Chymotrypsin dargestellt.In FIG. 4, the chymotrypsin is illustrated.
In der Fig. 5 ist Monoklonales Immunogenisches Chymotrypsin (MIC), das immunogenischen Peptiden 3 enthält, dargestellt.In FIG. 5 Monoclonal Immunogenisches chymotrypsin (MIC) is that contains immunogenic peptides 3, is shown.
In der Fig 6 sind Chymotrypsinogen und a-Chymotrypsin, und die Lage der immunogenischen Peptiden 3 dargestellt. 6 shows chymotrypsinogen and a-chymotrypsin, and the location of the immunogenic peptides 3 .
Die Bilder stammen aus dem Buch "Molecular Cell Biology" H. Lodish, A. Berk usw.The pictures come from the book "Molecular Cell Biology" H. Lodish, A. Berk etc.
Die Monoklonale Immunogenische Protease (MIP) in der Fig. 1. katalysiert die Spaltung einer bestimmten Peptidkette an ganz bestimmten Stellen. Diese Peptidkette ist das Antigen der immunogenischen Zonen 2 und/oder Peptiden 3 (Fig. 2) der Protease 1.The monoclonal immunogenic protease (MIP) in FIG. 1 catalyzes the cleavage of a specific peptide chain at very specific locations. This peptide chain is the antigen of the immunogenic zones 2 and / or peptides 3 ( FIG. 2) of the protease 1 .
Bei der Interaktion vom immunogenischen Peptid 3 und/oder immunogenischer Zone 2 mit dem Antigen, wird dieses in der Ort der Interaktion durch die Protease 1 gespaltet. Das Chymotrypsin in der Fig. 4 hydrolysiert hinter Phenylalanin, Tryptophan und Tyrosin, und besteht aus drei Ketten A, B und C, je 13, 131 und 97 Aminosäuren. When the immunogenic peptide 3 and / or immunogenic zone 2 interacts with the antigen, it is cleaved by the protease 1 at the site of the interaction. The chymotrypsin in FIG. 4 hydrolyzes behind phenylalanine, tryptophan and tyrosine, and consists of three chains A, B and C, each with 13, 131 and 97 amino acids.
Monoklonales Immunogenisches Chymotrypsin (MIC) in der Fig. 5 hat die gleiche Funktionen wie das Chymotrypsin in der Fig. 4, enthält immunogenische Peptide 3, die gegen ein bestimmtes Antigen gerichtet sind. Das Antigen ist eine (Poly)Peptidkette d. h. ein Protein, das bei der Interaktion mit dem immunogenischen Peptid 3 des Chymotrypsins (Fig. 4) durch das Chymotrypsin in der Ort der Interaktion gespaltet wird.Monoclonal immunogenic chymotrypsin (MIC) in FIG. 5 has the same functions as the chymotrypsin in FIG. 4, contains immunogenic peptides 3 which are directed against a specific antigen. The antigen is a (poly) peptide chain, ie a protein which, when interacting with the immunogenic peptide 3 of chymotrypsin ( FIG. 4), is cleaved by the chymotrypsin in the site of the interaction.
Die immunogenische Peptiden 3 liegen im Chymotrypsinogen in der Fig. 6 an der Stellen z. B. zwischen 12 und 13 aa und zwischen 220 aa oder 244 aa und 245 aa.The immunogenic peptides 3 are located in the chymotrypsinogen in FIG . B. between 12 and 13 aa and between 220 aa or 244 aa and 245 aa.
Das Präparat wird z. B. in das Gebiet der Entflammung injiziert.The preparation is e.g. B. injected into the area of ignition.
Claims (2)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
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| DE1998122406 DE19822406A1 (en) | 1998-05-19 | 1998-05-19 | Composition for treating cancer and other diseases caused by pathogenic proteins |
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| Application Number | Priority Date | Filing Date | Title |
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| DE1998122406 DE19822406A1 (en) | 1998-05-19 | 1998-05-19 | Composition for treating cancer and other diseases caused by pathogenic proteins |
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| DE19822406A1 true DE19822406A1 (en) | 1999-11-25 |
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Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE19953696A1 (en) * | 1999-11-09 | 2001-05-10 | Alexander Cherkasky | Selective non-peptidic proteolytic enzyme analogue useful for the dissolution of plaques and treatment of polypeptide mediated illnesses comprises proteolytic amino acid residues bonded to a carrier molecule |
| DE10133071A1 (en) * | 2001-07-07 | 2003-03-06 | Alexander Cherkasky | New compound containing protease and a recognition component, useful for treating diseases associated with specific proteins, e.g. multiple sclerosis |
| EP1361891A2 (en) | 2001-02-19 | 2003-11-19 | MERCK PATENT GmbH | Artificial fusion proteins with reduced immunogenicity |
| US8034766B2 (en) | 2006-10-27 | 2011-10-11 | E I Du Pont De Nemours And Company | Compositions and methods for prion decontamination |
| DE102012015806A1 (en) | 2012-08-10 | 2014-02-13 | Alexander Cherkasky | New fusion protein comprising patient-specific region, which is encoded by a nucleic acid sequence or nucleic acid sequences of at least one individual, preferably human, useful for treating e.g. cancer and autoimmune diseases |
-
1998
- 1998-05-19 DE DE1998122406 patent/DE19822406A1/en not_active Ceased
Non-Patent Citations (1)
| Title |
|---|
| NICHTS ERMITTELT * |
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE19953696A1 (en) * | 1999-11-09 | 2001-05-10 | Alexander Cherkasky | Selective non-peptidic proteolytic enzyme analogue useful for the dissolution of plaques and treatment of polypeptide mediated illnesses comprises proteolytic amino acid residues bonded to a carrier molecule |
| EP1361891A2 (en) | 2001-02-19 | 2003-11-19 | MERCK PATENT GmbH | Artificial fusion proteins with reduced immunogenicity |
| DE10133071A1 (en) * | 2001-07-07 | 2003-03-06 | Alexander Cherkasky | New compound containing protease and a recognition component, useful for treating diseases associated with specific proteins, e.g. multiple sclerosis |
| US8034766B2 (en) | 2006-10-27 | 2011-10-11 | E I Du Pont De Nemours And Company | Compositions and methods for prion decontamination |
| US8431526B2 (en) | 2006-10-27 | 2013-04-30 | E. I. Du Pont De Nemours And Company | Compositions and methods for prion decontamination |
| DE102012015806A1 (en) | 2012-08-10 | 2014-02-13 | Alexander Cherkasky | New fusion protein comprising patient-specific region, which is encoded by a nucleic acid sequence or nucleic acid sequences of at least one individual, preferably human, useful for treating e.g. cancer and autoimmune diseases |
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