CN116003511A - Morchella-derived hypoglycemic peptide and application thereof - Google Patents
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Abstract
本发明提供了羊肚菌源降血糖肽及其应用，属于生物医药技术领域。本发明提供了羊肚菌源降血糖肽，包括三肽和/或四肽；所述三肽的氨基酸序列为PTW，所述四肽的氨基酸序列为MPTW。本发明的羊肚菌源降血糖肽分子量均小于1000、疏水性强，含有Pro和Trp。分子对接结果表明：PTW和/或MPTW能与蛋白酶类糖尿病防治靶点二肽基肽酶IV、蛋白酪氨酸磷酸酶1B和α‑淀粉酶以氢键和疏水作用相结合发挥降血糖作用。且本发明的降血糖肽属于天然产物，无溶血性和致敏性，有较好的药代动力学特性。本发明对食源降血糖肽的开发具有一定指导意义。
The invention provides a morel-derived hypoglycemic peptide and an application thereof, belonging to the technical field of biomedicine. The present invention provides morel-derived hypoglycemic peptides, including tripeptides and/or tetrapeptides; the amino acid sequence of the tripeptide is PTW, and the amino acid sequence of the tetrapeptide is MPTW. The hypoglycemic peptide derived from hickory chick of the present invention has a molecular weight of less than 1000, strong hydrophobicity, and contains Pro and Trp. Molecular docking results show that PTW and/or MPTW can combine with protease-like diabetes prevention and treatment targets dipeptidyl peptidase IV, protein tyrosine phosphatase 1B and α-amylase to play a hypoglycemic effect by hydrogen bonding and hydrophobic interaction. Moreover, the hypoglycemic peptide of the present invention belongs to natural products, has no hemolysis and sensitization, and has good pharmacokinetic properties. The invention has certain guiding significance for the development of food-source hypoglycemic peptides.
Description
Technical Field
The invention belongs to the technical field of biological medicines, and particularly relates to Morchella-derived hypoglycemic peptide and application thereof.
Background
Diabetes (diabetes mellitus) is a series of metabolic disorders syndrome of proteins, fats and electrolytes caused by absolute or relative insufficient secretion of insulin and reduced sensitivity of target tissue cells to insulin. Diabetes has become a global public health problem. At present, clinically used medicines (such as the glucose, the linalool and the statin) can effectively control the blood sugar level of diabetics, but also cause a series of side effects (such as gastrointestinal diseases, diarrhea and the like), so the search for natural active ingredients with safety and small toxic and side effects for preventing and treating diabetes has become a research hotspot in the fields of food science and medicine in recent years.
The bioactive peptide has the advantages of simple structure, good safety, easy absorption, no immunoreactivity and the like, has good nutrition and functional characteristics, has various health benefits such as antioxidation, blood pressure reduction, blood sugar reduction and the like, and has good application prospect in the fields of functional foods and medicines. Currently, hundreds of hypoglycemic peptides have been isolated and prepared from different raw material protein hydrolysates, and food-borne hypoglycemic peptides are considered as a healthier potential alternative for the prevention and treatment of diabetes.
However, there is no report on Morchella-derived hypoglycemic peptides.
Disclosure of Invention
In view of the above, the present invention aims to provide a morchella-derived hypoglycemic peptide and application thereof, wherein the morchella-derived hypoglycemic peptide has good hypoglycemic activity.
The invention provides Morchella-derived hypoglycemic peptide, which comprises tripeptide and/or tetrapeptide; the amino acid sequence of the tripeptide is PTW, and the amino acid sequence of the tetrapeptide is MPTW.
The invention also provides application of the Morchella-derived hypoglycemic peptide in preparation of hypoglycemic products.
Preferably, the morchella-derived hypoglycemic peptide can exert the hypoglycemic effect by combining with a protease type diabetes prevention and treatment target.
Preferably, the protease type diabetes prevention and treatment target comprises one or more of dipeptidyl peptidase IV, protein tyrosine phosphatase 1B and alpha-amylase.
The invention also provides a blood sugar reducing product, which comprises the Morchella-derived blood sugar reducing peptide.
Preferably, the product comprises a food, a health product or a pharmaceutical product.
Preferably, the dosage form of the pharmaceutical product comprises an oral formulation.
The invention also provides application of the Morchella-derived hypoglycemic peptide in preparation of an enzyme inhibitor; the enzyme comprises one or more of dipeptidyl peptidase IV, protein tyrosine phosphatase 1B and alpha-amylase.
The invention provides Morchella-derived hypoglycemic peptide, which comprises tripeptide and/or tetrapeptide; the amino acid sequence of the tripeptide is PTW, and the amino acid sequence of the tetrapeptide is MPTW. The morchella-derived hypoglycemic peptide has the molecular weight of less than 1000, strong hydrophobicity and Pro and Trp. The molecular docking results indicate that: PTW and/or MPTW can play a role in reducing blood sugar by combining with key amino acid residues of protease diabetes prevention target dipeptidyl peptidase IV (DPP-4), protein tyrosine phosphatase 1B (PTP 1B) and alpha-amylase active centers through hydrogen bonds and hydrophobic effects. IC50 s of PTW for DPP4, PTP1B and alpha-amylase inhibition were 16.08.+ -. 1.11mM, 5.89.+ -. 0.21mM and 18.75.+ -. 0.43mM, respectively; the IC50 s of MPTW for DPP4, PTP1B and alpha-amylase inhibition were 6.34.+ -. 0.03mM, 3.06.+ -. 0.12mM and 14.59.+ -. 0.17mM, respectively. The hypoglycemic peptide belongs to a natural product, has no hemolysis and sensitization, and has better pharmacokinetic properties. The invention has certain guiding significance for developing food-source hypoglycemic peptide.
Drawings
FIG. 1 is a mass spectrum of PTW;
FIG. 2 is a mass spectrum of MPTW;
FIG. 3 is a 2D plot of MPTW and DPP-4 interactions;
FIG. 4 is a 2D diagram of MPTW and PTP1B interactions;
FIG. 5 is a 2D plot of MPTW and alpha-amylase interactions;
FIG. 6 is a 3D graph of MPTW and DPP-4 interactions;
FIG. 7 is a 3D diagram of MPTW and PTP1B interactions;
FIG. 8 is a 3D diagram of MPTW and alpha-amylase interactions;
FIG. 9 is a 2D graph of PTW and DPP-4 interactions;
FIG. 10 is a 2D diagram of PTW and PTP1B interactions;
FIG. 11 is a 2D graph of PTW and alpha-amylase interactions;
FIG. 12 is a 3D graph of PTW and DPP-4 interactions;
FIG. 13 is a 3D diagram of PTW and PTP1B interactions;
FIG. 14 is a 3D graph of PTW and alpha-amylase interactions;
the enzyme receptors in FIGS. 6-8 and 12-14 are represented in iridescent form by the carton format and the peptide ligands in yellow surface format; the green dotted lines in figures 3-5 and 9-11 represent hydrogen bonds,
representing a hydrophobic effect.
Detailed Description
The invention provides Morchella-derived hypoglycemic peptide, which comprises tripeptide and/or tetrapeptide; the amino acid sequence of the tripeptide is PTW, and the amino acid sequence of the tetrapeptide is shown as SEQ ID NO.1, specifically MPTW.
In the invention, the molecular weight of PTW and MPTW is less than 1000, the solubility is poor, the hydrophobicity is strong, the net charge is zero, and the isoelectric point is biased to acid; has no hemolysis and sensitization, and basically has no aggregation and immunogenicity. In addition, the hypoglycemic peptide PTW and MPTW have different oral bioavailability, are easy to be absorbed by intestinal tracts, and can penetrate through Caco-2 cells and blood brain barriers to different degrees; the induction rate to cytochrome P450 is less than 0.10, the inhibition rate is less than 0.40, and the inhibition rate to cytochrome P450 is lower, so that the inhibition rate to cytochrome P450 has lower human body clearance rate, and is indicated to have stronger metabolic stability; 2 peptides were essentially free of Ames toxicity and Hek293 cytotoxicity. PTW and MPTW have good pharmacokinetic properties.
In the present invention, PTW and MPTW are preferably obtained by solid phase synthesis. In the implementation of the invention, PTW and MPTW are obtained by solid phase synthesis from Shanghai Synpeptide Biotechnology company.
The invention also provides application of the Morchella-derived hypoglycemic peptide in preparation of hypoglycemic products.
In the invention, the Morchella-derived hypoglycemic peptide can play a role in reducing blood sugar by combining with a protease diabetes prevention and treatment target.
In the invention, the protease type diabetes prevention target preferably comprises one or more of DPP-4, PTP1B and alpha-amylase.
The invention also provides a blood sugar reducing product, which comprises the Morchella-derived blood sugar reducing peptide.
In the present invention, the product preferably includes food, health products or medicines.
In the present invention, the dosage form of the pharmaceutical product preferably includes an oral preparation.
The invention also provides application of the Morchella-derived hypoglycemic peptide in preparation of an enzyme inhibitor; the enzyme comprises one or more of DPP-4, PTP1B and alpha-amylase.
In the present invention, MPTW hydrogen bonds with Glu205, his740 and Arg125 of DPP-4, and hydrophobic interactions with Asn545, asn562, tyr (48,547,631,662,752), trp (563,627,629) and Ser 630; hydrogen-bonding to Glu200 of PTP1B, hydrophobic-bonding to Leu192, asn193, phe (196,280), lys197, arg199, gly277, and Glu 276; hydrogen-bonding to Thr163, asp197 of alpha-amylase and hydrophobic binding to Trp (58, 59), tyr62, gln63, arg195, glu233, phe256, asn298, his (299,305) and Asp (300,356).
PTW hydrogen bonds with Arg125, glu206 and Tyr662 of DPP-4, and hydrophobic interactions with Glu205, tyr (547,631,666), trp (629,659), val (656,711) and Ser 630; hydrogen-bonding to Glu115, trp179, arg221 and gin 262 of PTP1B, hydrophobic-bonding to Tyr46, lys120, gly183, val184, ala217, thr263, asp265 and gin 266; tyr62 and Asp300 bind to alpha-amylase by hydrogen bond, and bind to Trp (58, 59), gln63, thr163, leu165, arg195, asp197, glu233, his (101,299,305) and Asp356 by hydrophobic interaction.
In the present invention, the IC50 of PTW for DPP4, PTP1B and alpha-amylase inhibition is 16.08+ -1.11 mM, 5.89+ -0.21 mM and 18.75+ -0.43 mM, respectively; the IC50 s of MPTW for DPP4, PTP1B and alpha-amylase inhibition were 6.34.+ -. 0.03mM, 3.06.+ -. 0.12mM and 14.59.+ -. 0.17mM, respectively. PTW and MPTW have good inhibition effect on DPP-4, PTP1B and alpha-amylase.
The technical solutions of the present invention will be clearly and completely described in the following in connection with the embodiments of the present invention.
Example 1 Morchella-derived hypoglycemic peptide screening process and physicochemical properties thereof
The 154 Morchella major structural protein sequences were downloaded from the UniProt KB protein database (https:// www.uniprot.org /). These white sequences are preferably selected using the CALCULATIONS module (https:// biochem. Uwm. Edu. Pl/biocpep-uwm /) in the BIOPEPUWM database. The method comprises the following steps: the downloaded 154 Morchella protein sequences are respectively adhered to a CALCULATIONS module of a BIOPEPUWM database, analysis and operation are carried out, the Sigma A value (the occurrence frequency of the hypoglycemic peptide; the set ratio is 70%) and the Sigma B value (the potential hypoglycemic activity; the set ratio is 30%) are synthesized, and 20 Morchella proteins with higher scores are obtained through preliminary screening to be used as experimental research materials.
And performing virtual enzymolysis on the 20 primarily screened Morchella proteins through an 'ENZYME (S) ACTION' module in a BIOPEPUWM database. The 40S ribosomal protein S9 protein having the highest score is preferably obtained by integrating the Σae value (release frequency of the hypoglycemic peptide; 50% by weight) and the Σw value (relative release frequency of the hypoglycemic peptide; 50% by weight) as a raw material protein for producing the morchella-derived hypoglycemic peptide (table 1).
TABLE 1 optimization and virtual enzymatic hydrolysis results of Morchella proteins
The potential of the resulting peptide fragment for bioactivity was evaluated using a PeptideRanker (http:// distilldeep. Ucd. Ie/PeptideRanker /). The peptide fragments with PeptideRanker score greater than 0.5 were subjected to a second round of screening with iDPPIV-SC M (http:// camt. Pythonanywrere. Com/iDPPIV-SCM); in combination with the novel assay, 2 Morchella-derived hypoglycemic peptides PTW and MPTW (Table 2) were screened for a higher iDPPIV-SCM score and were not reported. Mass spectra corresponding to PTW and MPTW are shown in fig. 1 and 2, respectively.
Table 2 virtual screening of 2 Morchella-derived hypoglycemic peptides
The molecular weight, isoelectric point and solubility of the hypoglycemic peptide are predicted by Innovagen (http:// www.innovagen.com); pepdraw (http:// www.tulane.edu/-biochem/WW/PepDraw /) predicts net charge and hydrophobicity; allergyleab (https:// sortaller. Gzhmu. Edu. Cn /) predicts sensitization; hemoPI (https:// webs. Iiitd. Edu. In/raghava/hemapi/design. Php) predicts hemolysis; chemAGG (https:// admet. Scbdd. Com/ChemAGG/index /) predicts aggregation; IEDB (http:// tools. IEDB. Org/immunogenicity /) predicts immunogenicity. The physical and chemical property prediction results of the 2 Morchella-derived hypoglycemic peptides are shown in Table 3.
Table 3 physicochemical Properties of Morchella-derived hypoglycemic peptide
As can be seen from Table 3, the molecular weight of the Morchella-derived hypoglycemic peptides PTW and MPTW is less than 1000, the solubility is poor, the hydrophobicity is strong, the net charge is zero, and the isoelectric point is biased to be acidic; the morchella-derived hypoglycemic peptide has no hemolysis and sensitization, basically no aggregation and immunogenicity, and has good physicochemical property and safety.
Example 2 pharmacokinetics of Morchella-derived hypoglycemic peptide
The pharmacokinetic properties of the hypoglycemic peptides of the present invention were predicted by an iDrug (https:// drug. Ai. Tent. Com/con/cn/admet) tool and the results are shown in Table 4. It can be seen that the hypoglycemic peptides PTW and MPTW have different oral bioavailability, are easily absorbed by intestinal tracts, and can penetrate Caco-2 cells and blood brain barriers to different degrees; the induction rate to cytochrome P450 is less than 0.10, the inhibition rate is less than 0.40, and the inhibition rate to cytochrome P450 is lower, so that the inhibition rate to cytochrome P450 has lower human body clearance rate, and is indicated to have stronger metabolic stability; 2 peptides were essentially free of Ames toxicity and Hek293 cytotoxicity. In summary, the morchella-derived hypoglycemic peptide has good pharmacokinetic properties.
TABLE 4 pharmacokinetic property prediction results for hypoglycemic peptides
Note that: the solubility coefficient is the thermodynamic water solubility value of the substance, expressed in Log (S, mol/L); caco-2 cell permeability was CACO-2 permeability value (10 -6 cm/s); human clearance reflects the excretion of the test substance in the human body and is expressed by log10 (ml/min/kg); the other index corresponding data is a probability value (between 0 and 1).
Example 3 molecular docking of Morchella-derived hypoglycemic peptides
Molecular docking is a powerful tool for studying the interaction of polypeptides with target protein receptors. Docking studies were performed with the hpepdOCK tool (http:// huanglab. Phys. Hust. Edu. Cn/HPEPDOCK /) using the hypoglycemic peptide as ligand with possible protease-type diabetes control targets (DPP-4, PTP1B and alpha-amylase) and the docking scores are shown in table 5. As can be seen from Table 5, MPTW has the highest score of docking with 3 enzyme receptors and PTW also has a relatively high docking score.
Table 5 molecular docking results of Morchella-derived hypoglycemic peptides with DPP4, PTP1B and alpha-amylase
The molecular docking results of MPTW with 3 enzyme receptors are shown in FIGS. 3-8, wherein FIGS. 3, 4 and 5 show 2D interaction diagrams of MPTW with DPP-4, PTP1B and alpha-amylase respectively, FIGS. 6,7 and 8 show 3D interaction diagrams of MPTW with DPP-4, PTP1B and alpha-amylase respectively, and FIGS. 3-8 show that MPTW is hydrogen bonded with Glu205, his740 and Arg125 of DPP-4 and is hydrophobic bonded with Asn545, asn562, tyr (48,547,631,662,752), trp (563,627,629) and Ser 630; hydrogen-bonding to Glu200 of PTP1B, hydrophobic-bonding to Leu192, asn193, phe (196,280), lys197, arg199, gly277, and Glu 276; hydrogen-bonding to Thr163, asp197 of alpha-amylase and hydrophobic binding to Trp (58, 59), tyr62, gln63, arg195, glu233, phe256, asn298, his (299,305) and Asp (300,356).
The molecular docking results of PTW with 3 enzyme receptors are shown in FIGS. 9-14, wherein FIGS. 9, 10 and 11 are respectively 2D interaction diagrams of PTW with DPP-4PTP1B and alpha-amylase, FIGS. 12, 13 and 14 are respectively 3D interaction diagrams of PTW with DPP-4, PTP1B and alpha-amylase, and FIGS. 9-14 show that PTW is combined with Arg125, glu206 and Tyr662 of DPP-4 through hydrogen bonding and combined with Glu205, tyr (547,631,666), trp (629,659), val (656,711) and Ser630 through hydrophobic interaction; hydrogen-bonding to Glu115, trp179, arg221 and gin 262 of PTP1B, hydrophobic-bonding to Tyr46, lys120, gly183, val184, ala217, thr263, asp265 and gin 266; tyr62 and Asp300 bind to alpha-amylase by hydrogen bond, and bind to Trp (58, 59), gln63, thr163, leu165, arg195, asp197, glu233, his (101,299,305) and Asp356 by hydrophobic interaction.
The Morchella-derived hypoglycemic peptide of the invention can be combined with Glu (205, 206), tyr (547,631,662,666), ser630, val656, trp659, val711 and His740 of DPP-4, which are key amino acid residues in the enzyme activity pocket [1] The method comprises the steps of carrying out a first treatment on the surface of the Except for a few amino acids such as Trp179, gly183, val184, gln266 and Asp265, all other amino acid residues of Morchella-derived hypoglycemic peptide combined with PTP1B are identical to Ali [2] The reported results of the fucoidan quinone docking with PTP1B are the same; in addition, trp (58, 59), tyr62, gln63, thr163, arg195, asp197, glu233, his305, asp300 and the like, which are the binding peptides of Morchella-derived hypoglycemic peptides with alpha-amylase, are all important residues of the active center of the enzyme [3] 。
Example 4 hypoglycemic Activity of Morchella-derived hypoglycemic peptide
Using bodyExternal chemistry experiment model method [4-6] Inhibition of DPP-4, PTP1B and alpha-amylase by PTW and MPTW was evaluated (Table 6). It can be seen that PTW and MPTW have good inhibition on DPP-4, PTP1B and alpha-amylase.
TABLE 6 IC50 values for PTW and MPTW on DPP-4, PTP1B and alpha-amylase inhibition
Note that: the IC50 unit of Morchella-derived hypoglycemic peptide is mM, the IC50 unit of positive control vildagliptin is nM, and the IC50 unit of sodium orthovanadate and acarbose is μM.
Reference is made to:
[1].Zhao L,Zhang M,Pan F,Li J,Dou R,Wang X,Wang Y,He Y,Wang S,Cai S:In silico analysis of novel dipeptidyl peptidase-IV inhibitory peptides released from Macadamia integrifolia antimicrobial protein 2(MiAMP2)and the possible pathways involved in diabetes protection.Current research infood science 2021,4:603-611.
[2].Ali MY,Kim DH,Seong SH,et al.α-Glucosidase and protein tyrosine phosphatase 1B inhibitory activity of plastoquinones from marine brown alga Sargassum serratifolium.Marine drugs 2017,15(12):368.
[3].Khan M,Alam A,Khan KM,et al.Flurbiprofen derivatives as novel α-amylase inhibitors:Biology-oriented drug synthesis(BIODS),in vitro,and in silico evaluation.Bioorganic chemistry 2018,81:157-167.
[4] yang Zhenzhen the effect of three hypoglycemic plants from Xinjiang on dipeptidyl peptidase IV activity; 2012.
[5] niu Enli design, synthesis and in vitro inhibition activity study of sulfonamide protein tyrosine phosphatase 1B inhibitor; 2016.
[6].Cheng Q,Cai S,NiD,WangR,ZhouF,JiB,ChenY:Invitro antioxidantandpancreaticα-amylase inhibitory activity of isolated fractions from water extract of Qingzhuan tea.Journal of food science and technology2015,52(2):928-935.
although the foregoing embodiments have been described in some, but not all, embodiments of the invention, according to which one can obtain other embodiments without inventiveness, these embodiments are all within the scope of the invention.
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| CN115010785A (en) * | 2022-05-16 | 2022-09-06 | 江南大学 | Tetrapeptide with dipeptidyl peptidase-4 inhibitory activity and application thereof |
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| US20030119725A1 (en) * | 2000-07-31 | 2003-06-26 | Gilles Divita | Peptide-mediated transfection agents and methods of use |
| CN1724563A (en) * | 2005-06-29 | 2006-01-25 | 常州制药厂有限公司 | Exendin4 polypeptide fragment |
| US20200216504A1 (en) * | 2017-06-30 | 2020-07-09 | Universite De Strasbourg | Peptides for treatment and prevention of hyperglycaemia |
| CN115010785A (en) * | 2022-05-16 | 2022-09-06 | 江南大学 | Tetrapeptide with dipeptidyl peptidase-4 inhibitory activity and application thereof |
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