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

Synthesis method of cyclic pentapeptide and its application in anti-hepatitis C drugs

A cyclic pentapeptide and drug technology, applied to the cyclic pentapeptide and its application in anti-hepatitis C drugs, can solve the problems of disappearance, weakened antiviral efficacy, loss of internal binding ability of hydrophobic channels, etc., and achieves good structural stability, Efficient combination effect

Active Publication Date: 2022-05-31
TIANJIN MEDICAL UNIV
View PDF5 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, the actual synthesis research shows that due to the excessive tension inside the cyclic tetrapeptide structure, it is difficult to form a cyclized structure, and even after forming a cyclic structure, it may lose its binding ability in the hydrophobic channel due to the instability of the cyclized structure, resulting in Antiviral efficacy weakened or even disappeared

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
  • Synthesis method of cyclic pentapeptide and its application in anti-hepatitis C drugs
  • Synthesis method of cyclic pentapeptide and its application in anti-hepatitis C drugs
  • Synthesis method of cyclic pentapeptide and its application in anti-hepatitis C drugs

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0026] For better understanding of the present invention, the present invention will be described in detail below with reference to the specific drawings.

[0027] 1. Preparation of cyclic pentapeptides

[0028] 1.1 Raw materials and reagents:

[0029] (1) Protect amino acids and raw materials

[0030] Fmoc-Arg(Pbf)-OH, Fmoc-D-Tyr(tBu)-OH, Fmoc-Glu(OtBu)-OH, Fmoc-Asp(OtBu)-OH, etc.

[0031] (2) Condensation reagent

[0032] HBTU, DIEA,

[0033] (3) Solvent

[0034] DMF, DCM, acetonitrile,

[0035] (4) Resin

[0036] 2-Chlorotrityl chloride resin

[0037] (5) Deprotection reagent

[0038] piperidine

[0039] (6) Cutting reagent

[0040] Trifluoroethanol, DCM, TFA, TIS, EDT, H 2 O

[0041] (7) Nitrogen

[0042] (8) Anhydrous ether

[0043] (9) Precision electronic balance

[0044] 1.2 Synthesis process:

[0045] (1) Resin swelling

[0046] The 2-Chlorotrityl Chloride Resin resin was put into the reaction tube, DCM (15ml / g) was added, and it was shaken for 30min....

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 provides a cyclic pentapeptide, the amino acid sequence of which is: cyclic-5-aspartic acid-glutamic acid-arginine-tyrosine-arginine. The cyclic pentapeptide inhibitor provided by the invention has good structural stability, can be efficiently combined with p7 channel protein, and effectively exerts the anti-hepatitis C virus effect.

Description

technical field [0001] The invention belongs to the field of biotechnology, and relates to a novel cyclic pentapeptide and its application in anti-hepatitis C drugs. Background technique [0002] Studies have shown that p7 is an important protein that affects (hepatitis C virus) HCV infection activity. p7 exists in the endoplasmic reticulum, has cation transport activity, and has higher selectivity for calcium ions. It is the only ion channel protein in HCV. In the liposome ion flux experiment, inhibition of p7 protein can obviously block the ion flux on both sides of the membrane, and the p7 protein is knocked out or the mutation of p7 protein R33Q or R35Q is performed on the viral genome, and hepatitis C virus is in the extracellular supernatant. titers were significantly eliminated [1,2] . It is inferred from this that the p7 protein acts as an ion channel and then plays a function related to the release of HCV. Therefore, the p7 ion channel can be used as a good drug...

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
Patent Type & Authority Patents(China)
IPC IPC(8): C07K7/64A61K38/12A61P31/14
CPCC07K7/64A61P31/14A61K38/00Y02A50/30
Inventor 王树青董卫莉魏树琨欧阳波周界文
Owner TIANJIN MEDICAL 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