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

Peptide for preventing or treating liver damage

A technology for liver injury and acute liver injury, applied in the direction of peptides, peptide/protein components, medical preparations containing active ingredients, etc., can solve problems such as liver cell necrosis

Inactive Publication Date: 2011-09-14
程云 +1
View PDF7 Cites 7 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

As another example, long-term use of antibiotics such as rifampicin, pyrazinamide, and isoniazid, and long-term use of estrogen during menopause can also cause severe liver cell necrosis, leading to liver damage such as acute or chronic hepatitis, jaundice, and liver fibrosis

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
  • Peptide for preventing or treating liver damage
  • Peptide for preventing or treating liver damage
  • Peptide for preventing or treating liver damage

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 2

[0066] The preparation of embodiment 2 peptide conjugates

[0067] Peptide A was cross-linked with bovine serum albumin (BSA) to form a conjugate by the glutaraldehyde method. The specific conjugation process is as follows: Take 1 mg of the peptide A synthesized in Example 1 and dissolve it in 0.5 ml of PBS (pH7.4, 0.02mol / L); take 4.5 mg of BSA and dissolve it in 4.5 ml of PBS (pH7.4, 0.02 mol / L). Mix the above peptide A and BSA solutions, then slowly add 1 ml of 0.1% glutaraldehyde, and let the cross-linking reaction proceed for 12 hours at room temperature in the dark. Then glycine solution (1 mol / L) was slowly added to stop the reaction, followed by dialysis with PBS (pH 7.4, 0.02 mol / L) overnight and freeze-drying. The obtained cross-linked product of peptide A and BSA was named as peptide conjugate A.

Embodiment 3

[0068] Example 3 Peptide Reactivity Research with Hepatitis C Patient's Serum

[0069] 3.1 Serum source

[0070] Anti-HCV antibody positive serum: Randomly obtained from hospitalized patients with HCV infection in the 302 Hospital of the People's Liberation Army from 2000 to 2001.

[0071]Control serum: taken from healthy blood donors, and the results of laboratory tests showed that all indicators were normal.

[0072] Hepatitis B (HBV) patient serum: selected from patients inpatients with hepatitis B in the 302 Hospital of the People's Liberation Army, all of which were positive for hepatitis B virus surface antigen in laboratory tests.

[0073] 3.2 The method of detecting serum reactivity by indirect ELISA method

[0074] According to conventional indirect ELISA technology, DG3022 enzyme-linked immunoassay instrument (purchased from Perkin Elmer) was used to detect the reactivity of various peptides of the present invention with various sera. Add 10 μg each of peptide A, ...

Embodiment 4

[0079] Example 4 Peptide Immunogenicity in Mice and Research on Cytokine in Serum

[0080] 4.1 Experimental animals

[0081] BALB / c mice (all male, 6 weeks old, purchased from the Experimental Animal Center of the Academy of Military Medical Sciences, Beijing) were taken and divided into the following 4 groups, 5 mice in each group: (1) control group; (2) peptide A group ( (immunized with peptide A); (3) peptide B group (immunized with peptide B); (4) peptide C group (immunized with peptide C).

[0082] 4.2 Immunization method

[0083] The peptides (100 μg / μl) used in each group were mixed with 50 μl of complete Freund’s adjuvant (GIBCOBRL company) in equal volumes, fully mixed with a micro-stirrer, and injected into the foot pads of mice, thus completing the first treatment of mice. Immunization. Booster immunization was carried out 14 days later, 50 μl each of the peptide (100 μg / μl) and Freund’s incomplete adjuvant (GIBCOBRL) used in each group were immunized in the same...

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 relates to application of a peptide containing a sequence as shown in a formula I or a derivant thereof in preventing or treating liver damage, in particular to application of the peptide or the derivant thereof in preventing or treating the liver damage and hepatitis C. The formula I is as follows: Xaa1-Gln-Xaa2-Xaa3-Thr-Ser-Gly-Xaa4, wherein Xaa1 is deficiency, Ala, Gly, Val and Leu or Ile; Xaa2 is Thr or Ser; Xaa3 is Tyr and Phe or Trp; and Xaa4 is deficiency, Ala, Gly, Val, Leu and Ile or Pro. The invention also relates a medicine composite containing the peptide or the derivant thereof, a preparation method thereof and polynucleotide coding the peptide.

Description

field of invention [0001] The present invention relates to the use of hepatitis C virus immunogenic peptides and derivatives thereof for the prevention or treatment of liver damage, in particular to the use of the peptides or derivatives thereof in the prevention or treatment of immune liver damage and liver damage caused by hepatotoxic chemicals and its use in the prevention or treatment of hepatitis C. The present invention also relates to a pharmaceutical composition containing the peptide or its derivative, a preparation method and a polynucleotide encoding the peptide. Background technique [0002] Viral hepatitis is a serious disease that endangers human health, and its pathogen is a class of hepatropic viruses with different structures. So far, seven types of hepatitis viruses have been discovered, which are HAV, HBV, HCV, HDV, HEV and possibly TTV and HGV. Among them, hepatitis C virus (HCV) is the pathogen that causes hepatitis C. Hepatitis C was originally calle...

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 Applications(China)
IPC IPC(8): A61K38/08C07K7/06A61P1/16
Inventor 程云虞瑞鹤赵万洲赵军李靖
Owner 程云
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