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

Application of recombinant FN heparin binding domain polypeptide on preparing medicament resisting invasion and metastasis of malignant tumor

A heparin-binding domain, malignant tumor technology, applied in anti-tumor drugs, drug combinations, pharmaceutical formulations, etc., to achieve the effects of promoting angiogenesis, enhancing cell adhesion and proliferation, and enhancing activity

Active Publication Date: 2009-12-09
FUJIAN MEDICAL UNIV UNION HOSPITAL
View PDF1 Cites 1 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

The effect of recombinant FN N-terminal and C-terminal heparin-binding domain peptides on the invasion and metastasis of malignant tumors has never been reported

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
  • Application of recombinant FN heparin binding domain polypeptide on preparing medicament resisting invasion and metastasis of malignant tumor
  • Application of recombinant FN heparin binding domain polypeptide on preparing medicament resisting invasion and metastasis of malignant tumor
  • Application of recombinant FN heparin binding domain polypeptide on preparing medicament resisting invasion and metastasis of malignant tumor

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0045] The present invention is described in detail below in conjunction with accompanying drawing and embodiment:

[0046] The injection of mouse melanoma cell B16 cells into mice is used as an example below to illustrate that the recombinant FN heparin-binding domain polypeptide can be used in the preparation of drugs against invasion and metastasis of malignant tumors.

[0047] (1) Materials and reagents

[0048] 1. Main reagents

[0049] Native full-length fibronectin (FN): Purified from normal human plasma by gelatin affinity chromatography.

[0050] Recombinant FN polypeptide: recombinant FN N-terminal heparin-binding domain polypeptide (rhFNHN-29), recombinant FN C-terminal heparin-binding domain polypeptide (rhFNHC-36): the present invention constructs two heparin-binding domain polypeptides of FN N-terminus and C-terminus for yeast expression Vectors pPIC9K-rhFNHN-29, pPIC9K-rhFNHC-36, and high-expression yeast expression strains were screened out, rhFNHN-29 polypep...

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 an application of recombinant FN heparin binding domain polypeptide on preparing medicaments resisting the invasion and the metastasis of malignant tumors. The recombinant FN heparin binding domain polypeptide comprises five I type homologous structures at the end N in FN molecules and contains 237 amino acids in Ser46-Gly 282. DNA sequences for encoding the polypeptide range from 403bp to 1113bp and have the length of 711bp, a PCR amplified fragment has the length of 741bp, and the length of the fragment after double enzyme digestion is 729bp. The molecular weight of the polypeptide expressed by yeast is 28.52kDa, and the polypeptide comprises three III type homologous structures in the FN molecules, i.e. III-12, III-13 and III-14 and contains 272 amino acids in Tyr1720-Tyr1991. DNA sequences for encoding the polypeptide range from 5428bp to 6244bp and have the length of 816bp, a PCR amplified fragment has the length of 835bp, and the length of the fragment after double enzyme digestion is 828bp. The molecular weight of the polypeptide expressed by the yeast is 36.09kDa. The experiments prove that the recombinant FN heparin binding domain polypeptide can be applied to preparing medicaments resisting the invasion and the metastasis of malignant tumors.

Description

Technical field: [0001] The invention relates to the field of medicine, in particular to the application of recombinant fibronectin N-terminal and C-terminal heparin-binding domain polypeptides in the preparation of drugs for resisting invasion and metastasis of malignant tumors. Background technique: [0002] Fibronectin, fibronectin, hereinafter referred to as FN; invasion and metastasis are the biological characteristics of malignant tumors. In the invasion and metastasis of tumor, the adhesion and dissociation between tumor cells and tumor cells, tumor cells and vascular endothelial cells and extracellular matrix play an important role in the metastasis and spread. In recent years, how the components of the extracellular matrix in tumors affect the adhesion and migration of tumor cells, thereby affecting the invasion and metastasis of tumors has become a research hotspot. FN is an important component of the extracellular matrix (ECM). It is a glycoprotein macromolecule ...

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
IPC IPC(8): A61K38/16A61P35/00
Inventor 陈元仲黄涛邹起练陈显凌
Owner FUJIAN MEDICAL UNIV UNION HOSPITAL
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