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

Short peptide and immunosuppressant containing the same and application

An immunosuppressant and short peptide technology, which is applied in the field of medicine, can solve the problems of difficult production, high production cost, and high price, and achieve the effect of short structure, low side effects, and inhibition of binding

Inactive Publication Date: 2012-10-10
RUIJIN HOSPITAL AFFILIATED TO SHANGHAI JIAO TONG UNIV SCHOOL OF MEDICINE +1
View PDF0 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0007] Therefore, the technical problem to be solved by the present invention is to provide a new drug for the treatment of autoimmune diseases in view of the existing problems of difficult production, high production cost and high price in the existing drugs for treating autoimmune diseases produced by antibodies , the drug can specifically antagonize the interaction between FcγRIIA and IgG, thereby preventing or treating autoimmune diseases caused by antibodies

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
  • Short peptide and immunosuppressant containing the same and application
  • Short peptide and immunosuppressant containing the same and application
  • Short peptide and immunosuppressant containing the same and application

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0023] Design and synthesis of embodiment 1 short peptide sequence

[0024] After sequence design, optimization and screening, 9 short peptides were obtained, as shown in Table 1. Sent to Shanghai Jier Biochemical Synthesis, all with a purity >95%, for the tests in the following examples.

[0025]Table 1. Short peptides obtained through design and optimization

[0026]

Embodiment 2

[0027] Example 2 The short peptide compound of the present invention specifically antagonizes the interaction between FcγRIIA and IgG

[0028] The short peptides used are: No. 1-5 short peptides.

[0029] (1) Cell culture

[0030] U937 cells (purchased from the Cell Bank of the Chinese Academy of Sciences in Shanghai), using RMPI1640 culture medium containing 10% (v / v) calf serum, at 37 ° C, 5% (v / v) CO 2 to cultivate. K562 cells (purchased from Shanghai Chinese Academy of Sciences Cell Bank), using IMDM medium containing 10% (v / v) fetal bovine serum, 100 U / ml penicillin and 100 μg / ml streptomycin, at 37 ° C, 5% (v / v )CO 2 to cultivate.

[0031] (2) Determination of the activity of short peptide compounds to antagonize FcγRIIA-IgG interaction

[0032] The binding of FcγR and IgG on the cell surface was counted by flow cytometry.

[0033] Specific steps: Take cells in the doubling phase, wash 3 times with sterile PBS, and resuspend to 1×10 6 / ml. In the negative control...

Embodiment 3

[0040] Example 3 The short peptide can antagonize the binding between FcγRIIA-IgG in a concentration-dependent manner

[0041] The short peptide used is peptide No. 1.

[0042] (1) Cell culture

[0043] K562 cells were cultured in IMDM medium containing 10% (v / v) fetal bovine serum, 100 U / ml penicillin and 100 μg / ml streptomycin at 37°C in 5% (v / v) CO 2 to cultivate.

[0044] (2) CELL ELISA verification of short peptide concentration-dependent antagonism between FcγRIIA-IgG 96-well plate with 2% (w / v) PBS-B (2% (w / v) PBS-B, using 2g of bovine serum Albumin (BSA) was dissolved in 100ml PBS, similar to the following) to block, overnight at 4°C or 2h at room temperature. K562 cells in the logarithmic growth phase were washed 3 times with 1% (w / v) PBS-B. Resuspend K562 cells in 1% (w / v) PBS-B, adjust the concentration to 6×10 6 / ml, add 100 μl of K562 cells to each well, and remove the supernatant after centrifugation. The IgG group was directly added with a concentration gr...

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 a short peptide and an immunosuppressant containing the same and an application. The short peptide contains 6 peptides, and the amino acid sequence thereof is His-Pro-Ala-Pro-Ile-Phe. The short peptide can be used for preparing medicine for resisting the mutual action of an FcgammaIIA receptor (FcgammaRIIA) and immunoglobulin G (IgG) and for treating and preventing autoimmune diseases, and has the advantages of strong specificity, short structure, low immunogenicity and simple synthesis. The medicine with the short peptide can specifically resist the mutual action between FcgammaRIIA and IgG, but not resist the action between FcgammaRI and IgG, thereby having low side effect; the peptide will be widely applied in preparing novel immunosuppressant, and will bring huge social and economic benefits.

Description

[0001] This application is a divisional application of a patent application with an application date of April 24, 2009, an application number of 200910049954.0, and an invention title of "a short peptide, an immunosuppressant containing it and its application". technical field [0002] The invention belongs to the field of medicine, and in particular relates to a short peptide, an immunosuppressant containing it and application thereof. Background technique [0003] Antibody-generated autoimmune diseases are a type of autoimmune diseases that cause tissue and cell damage due to the production of autoantibodies. It includes a variety of diseases, such as the more common systemic lupus erythematosus, rheumatoid arthritis, multiple sclerosis, and anti-neutrophil antibody (Anti-Neutrophil Cytoplasmic Antibody, ANCA) associated small vessel inflammation. These diseases are a class of chronic progressive diseases with poor prognosis. In recent years, the pathogenesis of autoimmun...

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): C07K7/06A61K38/08A61P37/06
Inventor 陈楠张骥朱维良王伟铭俞海瑾陈永熙
Owner RUIJIN HOSPITAL AFFILIATED TO SHANGHAI JIAO TONG UNIV SCHOOL OF MEDICINE
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