Polypeptide with CXCR4 protein agonizing activity and application and medicinal composition thereof

A mixture and pharmaceutical technology, applied in the field of polypeptides with CXCR4 protein agonistic activity and their applications and pharmaceutical compositions, can solve the problems of lack of treatment methods

Active Publication Date: 2017-11-07
黄子为
View PDF9 Cites 2 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Neurological diseases such as multiple sclerosis, Alzheimer's disease, Parkinson's disease, Sandhoff disease, Tay-Sachs disease and stroke still lack effective treatments

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
  • Polypeptide with CXCR4 protein agonizing activity and application and medicinal composition thereof
  • Polypeptide with CXCR4 protein agonizing activity and application and medicinal composition thereof
  • Polypeptide with CXCR4 protein agonizing activity and application and medicinal composition thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0083] Example 1: Synthesis of H0001

[0084] Adopt Fmoc solid-phase synthesis method to synthesize, and concrete preparation method is as follows:

[0085] Weigh 357mg of Rink Amide-MBHA resin with a substitution degree of 0.28mmol / g in a solid phase reactor, add DCM to swell for 30min, then add 20% PIP / DMF solution for deprotection twice, the first time is 5min, and the second time is 20min . Wash several times with DCM and DMF respectively, and drain. It was detected by Kaiser test, and the resin or solution showed blue color, indicating that it had been deprotected.

[0086] Add Fmoc-D-Pro-OH (169mg, 0.5mmol), DIC (103mg, 0.5mmol), HOBt (68mg, 0.5mmol), DMF (4mL) into the solid phase reactor, and react at room temperature for 2h. After the coupling is completed, wash with DCM and DMF several times, and drain. Then use the Kaiser test to detect, and proceed to the next step after the detection is passed. Wash and dry the resin to obtain Fmoc-Pro-Rink Amide-MBHA resin. ...

Embodiment 2

[0089] The synthesis of embodiment 2 H0006

[0090] Weigh 357mg of Rink Amide-MBHA resin with a substitution degree of 0.28mmol / g in a solid phase reactor, add DCM to swell for 30min, then add 20% PIP / DMF solution for deprotection twice, the first time is 5min, and the second time is 20min . Wash several times with DCM and DMF respectively, and drain. It was detected by Kaiser test, and the resin or solution showed blue color, indicating that it had been deprotected.

[0091]Add Fmoc-Lys(Dde)-OH (266mg, 0.5mmol), DIC (103mg, 0.5mmol), HOBt (68mg, 0.5mmol), DMF (4mL) into the solid phase reactor, and react at room temperature for 2h. After the coupling is completed, the resin is washed and dried to obtain Fmoc-Lys(Dde)-Rink Amide-MBHA resin. The Kaiser test is used for detection, and the next reaction is carried out after the detection is passed. Add 20% PIP / DMF solution for deprotection twice, the first time is 5 minutes, the second time is 20 minutes, and the Fmoc protect...

Embodiment 3

[0096] Embodiment 3: polypeptide compound of the present invention

[0097] The amino acid sequence of the CXCR4 activity regulating polypeptide is shown in Table 1, and was synthesized according to the method described in Example 1 or Example 2.

[0098] Table 1 CXCR4 activity regulating polypeptide and its amino acid sequence

[0099]

[0100] a Italics represent D-type amino acids

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 the technical field of biological medicines, in particular to polypeptide with CXCR4 protein agonizing activity and application and a medicinal composition thereof. Fragments in the polypeptide are selected from polypeptide sequences which are derived from vMIP-II and formed through arbitrary arrangement of 3 amino acids to a full-length sequence, and selected from polypeptide sequences which are derived from SDF-1alpha(CXCL12) and formed through arbitrary arrangement of 3 amino acids to a full-length sequence. The polypeptide can effectively induce migration of SupT1 cells, and after being combined with CXCR4, the polypeptide can initiate an increase in intracellular calcium flow, which indicate that the polypeptide has the CXCR4 protein agonizing activity and can be used as a CXCR4 protein agonist.

Description

technical field [0001] The invention relates to the technical field of biomedicine, in particular to a polypeptide with CXCR4 protein activating activity and its application and pharmaceutical composition. Background technique [0002] Chemokine receptor CXCR4 belongs to the G protein-coupled receptor (G-protein-coupled receptor, GPCR) superfamily. Similar to other G protein-coupled receptors, CXCR4 consists of an extracellular N-terminus, seven transmembrane helices, three extracellular loop regions connecting the transmembrane helices, three intracellular loop regions, and an intracellular C-terminus. Unlike other chemokine receptors, only two endogenous natural ligands of CXCR4 have been found, namely chemokine stromal cell-derived factor (SDF-1α, CXCL12) and ubiquitin. After SDF-1α binds to the receptor CXCR4, it can activate multiple downstream signaling pathways, mediate cell proliferation, migration, homing, memory and transport of hematopoietic and lymphoid stem cel...

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): C07K19/00G01N33/68G01N33/574A61K38/19A61P25/28A61P25/00A61P35/00A61P37/00A61P31/18
CPCA61K38/00C07K14/522C07K2319/00G01N33/574G01N33/68
Inventor 黄子为
Owner 黄子为
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products

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

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap