Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Oligopeptide containing Hyp-Gly sequence and having antiplatelet and antithrombotic functions

An oligopeptide and sequence technology, applied in the fields of functional food and biomedicine, can solve the problems of high bleeding risk and increase bleeding events, and achieve the effects of prolonging bleeding time, easy absorption of enzymatic hydrolysis and inhibiting thrombosis.

Active Publication Date: 2020-09-11
CHINA AGRI UNIV
View PDF6 Cites 3 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0005] At present, although the oligopeptides derived from collagen GPR, GPRG, GPRGP, GPRPP and GPRPPP have inhibitory effects on ADP-induced human and rat platelet aggregation in vitro, the target of the GPR sequence polypeptide is the integration Inhibiting the activation of integrin receptor αIIbβ3, which is the final pathway of platelet activation and aggregation, leads to a higher risk of bleeding and increases the occurrence of bleeding events

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Oligopeptide containing Hyp-Gly sequence and having antiplatelet and antithrombotic functions
  • Oligopeptide containing Hyp-Gly sequence and having antiplatelet and antithrombotic functions
  • Oligopeptide containing Hyp-Gly sequence and having antiplatelet and antithrombotic functions

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0078] Example 1. Synthesis and functional verification of oligopeptides containing OG sequences

[0079] 1. Synthesis of oligopeptides containing OG sequence

[0080] The following peptides were synthesized: Pro-Gly-Glu-Hyp-Gly-Glu (PGEOGE), Glu-Hyp-Gly-Glu (EOGE), Hyp-Gly-Arg (OGR), Hyp-Gly-Ser-Glu (OGSE), Hyp-Gly-Glu (OGE), Hyp-Gly-Ser-Ala (OGSA), Arg-Hyp-Gly-Glu (ROGE), Hyp-Gly-Gln (OGQ), Pro-Gly-Glu-Hyp-Gly ( PGEOG), Gly-Glu-Hyp-Gly (GEOG), Hyp-Gly-Hyp-Met-Gly (OGOMG), Hyp-Gly-Glu-Phe-Gly (OGEFG).

[0081] The above 12 were synthesized by "Zhejiang Hongtuo Technology Co., Ltd." by solid-phase peptide synthesis, and the purity of the compound was verified by mass spectrometry to be greater than 98%. The result is given by figure 1 shown.

[0082] The oligopeptide solution containing the OG sequence is composed of the oligopeptide containing the OG sequence and a solvent, the solvent is deionized water, and the concentration of the solution is 10 mM (the concentration o...

Embodiment 2

[0113] Embodiment 2, prepare silver carp skin antiplatelet oligopeptide

[0114] One, utilize alkaline protease and trypsin to prepare the method for silver carp skin antiplatelet oligopeptide

[0115] 1. Preparation of collagen hydrolyzate containing OG sequence oligopeptide

[0116] (1) Extraction of silver carp skin gelatin:

[0117] After the silver carp skin is thawed, remove the scales, subcutaneous fat and muscle tissue on the surface, and rinse it with tap water. Cut the fish skin into about 0.5cm 2 Small pieces of small size, soaked in 0.05mol / L NaOH aqueous solution (material-to-liquid ratio 1:6, mass w / volume v) for 1 hour to remove fat and miscellaneous proteins, after soaking, rinse with tap water until neutral or slightly alkaline properties, to obtain the pretreated fish skin.

[0118] With 0.2% (v / v volume percentage) of H 2 SO 4 Soak the pretreated fish skin in the solution (ratio of solid to liquid: 1:6, w / v) for 1 hour to make it fully swell. After soa...

Embodiment 3

[0143] Embodiment 3, preparation Atlantic salmon fish skin antiplatelet oligopeptide

[0144] One, utilize alkaline protease and trypsin to prepare the method for Atlantic salmon fish skin antiplatelet oligopeptide

[0145] (1) Extraction of Atlantic salmon skin gelatin:

[0146] Same as the one of embodiment 2.

[0147] (2) Two-step enzymatic hydrolysis method to prepare gelatin hydrolyzate:

[0148] The first step of enzymatic hydrolysis: mix the gelatin prepared in the above (1) with water according to 6% (w / v) evenly, place the mixed solution in a water bath at 90°C for 10 minutes, pasteurize it, and after cooling, obtain sterilized Post gelatin solution.

[0149] Then use 1mol / L NaOH to adjust the gelatin solution to pH = 8.0, then add alkaline protease according to the mass ratio of enzyme to substrate 2%, and enzymolyze at 60°C for 4 hours to obtain the first-step enzymatic hydrolysis solution.

[0150] The second step of enzymatic hydrolysis: adjust the pH value of...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

No PUM Login to View More

Abstract

The invention discloses an oligopeptide containing an Hyp-Gly sequence and having antiplatelet and antithrombotic functions. The invention provides the oligopeptide containing the Hyp-Gly sequence orsalt forms thereof. The oligopeptide containing an OG sequence can be prepared through artificial synthesis as well as enzymolysis of fish skin. The molecular weight of the oligopeptide containing theOG sequence is smaller than 1,000 Da, the mass ratio of the oligopeptide to total enzyme-digested products is 65%-95%, and the oligopeptide has a specific inhibition effect on ADP-induced platelet aggregation, can inhibit thrombosis, does not affect the blood coagulation function, does not prolong the bleeding time and is very small in bleeding risk; and the oligopeptide has the characteristics of resistance to gastrointestinal tract digestive enzyme enzymolysis and easiness in absorption.

Description

technical field [0001] The invention belongs to the field of biomedicine and also belongs to the field of functional food (health food), and specifically relates to a class of oligopeptides with anti-platelet and antithrombotic functions containing Hyp-Gly sequence. Background technique [0002] The output of China's aquatic products accounts for about one-third of the world's total output, but the processing rate is about 30%, which is far behind that of developed countries such as the United States. The processing and comprehensive utilization technologies of aquatic products need to be further improved. At present, the utilization rate of by-products of aquatic product processing in my country is low, while foreign countries have achieved effective classification and utilization according to the chemical composition and biochemical characteristics of by-products, and the processing output value is even several to dozens of times higher than that of fish. In the process of...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
IPC IPC(8): C07K7/06C07K5/097C07K5/103C07K5/113C07K5/11C12P21/06A61K38/08A61K38/06A61K38/07A61P7/02A61P9/10
CPCC07K7/06C07K5/1021C07K5/1019C07K5/1008C07K5/0821C12P21/06A61P7/02A61P9/10A61K38/00
Inventor 李博田淇杨毅杰王博宋洪东
Owner CHINA AGRI UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com