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

Polypeptides regulating fgfr1 activity and applications thereof

An active, R1-P1 technology, applied in the direction of peptides, non-central analgesics, bone diseases, etc., can solve the problems of not being able to meet the medical needs of patients, and achieve good application value, low immunogenicity, and small molecular weight.

Active Publication Date: 2018-06-12
THE THIRD AFFILIATED HOSPITAL OF THIRD MILITARY MEDICAL UNIV OF PLA
View PDF3 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, whether it is drug treatment or surgical treatment, there are varying degrees of defects, which cannot meet the medical needs of patients.

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
  • Polypeptides regulating fgfr1 activity and applications thereof
  • Polypeptides regulating fgfr1 activity and applications thereof
  • Polypeptides regulating fgfr1 activity and applications thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0018] Example 1. Panning a polypeptide that can specifically bind to FGFR1 from a phage 12 peptide library

[0019] 1. Panning of phage 12 peptide library

[0020] Coat the microtiter plate with 150 μL of FGFR1 solution with a concentration of 20 μg / mL (sodium bicarbonate solution with a concentration of 0.1 mol / L and a pH of 8.6 as a solvent), coat at 4°C overnight, discard the coating solution, and fill the wells Add BSA solution with a concentration of 5 mg / mL (sodium bicarbonate solution with a concentration of 0.1 mol / L and a pH of 8.6 as a solvent), block at 37°C for 1 h, discard the blocking solution, and use TBST (that is, TBS containing Tween-20 buffer, the concentration of Tween-20 during the first round of panning was 1mL / L, and the concentration of Tween-20 was increased to 5mL / L during the second round and the third round of panning), washed 6 times, and dropped into phage (first round The mixture of phage 12 peptide library stock solution and TBST was put into ...

Embodiment 2

[0030] Example 2. Artificial synthesis of polypeptides that can specifically bind to FGFR1

[0031] According to the amino acid sequence of the R1-P1 peptide, Shanghai Qiangyao Biotechnology Co., Ltd. was entrusted to use the standard Fmoc protocol to synthesize the R1-P1 peptide in solid phase. It has been determined that the purity of the synthetic polypeptide is higher than 95%, and it is stored at -70°C.

Embodiment 3

[0032] Example 3, ELISA method to verify the combination of synthetic polypeptide and FGFR1

[0033]In a 96-well ELISA plate, add 20 μL of R1-P1 peptide solution with a concentration of 1 mmol / μL and coating buffer (take 0.3 g of sodium carbonate, 0.58 g of sodium bicarbonate and 0.04 g of sodium azide, dissolve in water, Adjust the pH to 9.6, then add water to dilute to 200mL to obtain) 80μL, set up a blank control group (without adding R1-P1 peptide), coat overnight at 4°C, discard the solution, and add a concentration of 50g / L small Bovine serum solution (PBS with pH 7.4 as solvent), blocked at 37°C for 60 min, discarded the solution, washed 3 times with PBST (PBS containing Tween-20 at a concentration of 0.5 mL / L, pH 7.4), and added a concentration of 30 μL of 100 μg / mL FGFR1 solution and 70 μL of PBS with a pH of 7.4 were incubated at 37°C for 1 h, washed 3 times with PBST, and a 1:500 dilution of mouse anti-FGFR1 antibody was added (1% BSA solution with a mass percent co...

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 polypeptide R1-P1 for adjusting FGFR1 (Fibroblast Growth Factors Receptor 1) activity. The polypeptide can be combined with the FGFR1 specificity, has an obvious adjusting function for the FGFR1 activity and can obviously restrain the activity of p-ERK in the main downstream signal path MAPK of FGFR1; after the R1-P1 peptide is articular injected to DMM model mouse, the regression of cartilago articularis and the loss level of matrix are obviously reduced; the process of arthritis is delayed. The polypeptide has the advantages of small molecular weight, simple preparation, controllable quality, low immunogenicity, and the like, can be used for preparing the drugs for relieving or treating osteoarthritis and has an excellent potential application value.

Description

technical field [0001] The invention belongs to the field of biotechnology, and in particular relates to a polypeptide R1-P1 regulating FGFR1 activity and its application in the preparation of medicines for alleviating or treating osteoarthritis. Background technique [0002] Osteoarthritis (OA) is a disease characterized by the degeneration, degeneration and secondary cartilage hyperplasia of articular cartilage, ossification as the main pathological change, and joint pain and activity dysfunction as the main clinical manifestations. It is a disease that seriously affects national health. major public health issues and quality of life. At present, there is no effective treatment for articular cartilage degeneration. Sodium hyaluronate and glucosamine are mainly used clinically to nourish and lubricate joints to relieve symptoms, but they cannot fundamentally inhibit the process of cartilage degeneration. Arthritis develops to the late stage, often take arthroscopic joint d...

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): C07K7/08A61K38/10A61P19/02A61P29/00
Inventor 陈林谭乔燕金旻杜晓兰王晓凤王权徐伟王先行
Owner THE THIRD AFFILIATED HOSPITAL OF THIRD MILITARY MEDICAL UNIV OF PLA
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