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

MUC1 tandem repeat sequences polypeptide, preparation technique thereof and use as anti-tumor medicament

A tandem repeat sequence and tandem repeat technology, applied in the field of tumor treatment, can solve the problems of limiting Th1 activation, tumor cell escape from the immune system, and direct effects that have not been reported in the literature to achieve the effect of inhibiting proliferation and growth

Inactive Publication Date: 2009-04-22
台桂香
View PDF0 Cites 5 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

The study found that tumor-derived soluble MUC1 could not be presented by DC cells, limiting the activation of Th1, thereby allowing tumor cells to escape the surveillance of the immune system
After searching relevant technical literature, there is no literature report on the direct effect of MUC1 polypeptide on tumor cells

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
  • MUC1 tandem repeat sequences polypeptide, preparation technique thereof and use as anti-tumor medicament
  • MUC1 tandem repeat sequences polypeptide, preparation technique thereof and use as anti-tumor medicament
  • MUC1 tandem repeat sequences polypeptide, preparation technique thereof and use as anti-tumor medicament

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0064] Synthesis of MUC1 tandem repeat polypeptide

[0065] A cDNA fragment of 1 to 10 tandem repeat sequences composed of 20 amino acid APDTRPAPGSTAPPAHGVTS of MUC1 tandem repeat sequence polypeptide was used to connect into pGEX-4T-1 vector, and then the recombinant plasmid was transformed into Escherichia coli DH5α. Transformed colonies were screened with ampicillin, and insert fragments were analyzed by enzyme digestion and gene sequencing. The recombinant plasmid was transformed into Escherichia coli DH5α, the expression was induced by 0.3mM IPTG, and the stable expression strain pGEX-MUC1 / DH5α was obtained by screening. A small amount of bacteria was boiled and lysed, the expression of MUC1-GST fusion protein was analyzed by 10% SDS-PAGE, and specific expression bands were identified by Western blotting. A large number of engineered bacteria were cultivated, and the supernatant was collected after sonication to purify human MUC1-GST fusion protein through Glutathione--S...

Embodiment 2

[0067] Synthesis of MUC1 tandem repeat polypeptide

[0068] Using the cDNA fragment of 1-10 tandem repeat sequences composed of 20 amino acid PPAHGVTSAPPDTRPAPGSTA of the MUC1 tandem repeat sequence polypeptide, the MUC1 polypeptide was synthesized according to the process described in Example 1, and made into a pharmaceutical preparation.

Embodiment 3

[0070] Synthesis of MUC1 tandem repeat polypeptide

[0071] Using the cDNA fragment of 1-10 tandem repeat sequences composed of 20 amino acids of the MUC1 tandem repeat sequence polypeptide DTRPAPGSTAPPAHGVTSAP, the MUC1 polypeptide was synthesized according to the process described in Example 1, and made into a pharmaceutical preparation.

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 provides polypeptide with tandem repeat sequences for MUC1 and a preparation technology and application as an anti-tumor drug thereof. Tandem repeat sequences of 20 amino acids of the MUC1 are adopted, cDNA fragments of 1 to 10 tandem repeat sequences are selected to link into a pGEX-4T-1 carrier, and a recombinant plasmid is transformed into colon bacillus DH5 alpha. A colony is transformed through the screening of penbritin, and the fragments are inserted through enzyme digestion and gene sequencing analysis. The recombinant plasmid is transformed into the colon bacillus DH5 alpha which is inducedly expressed through 0.3mM IPTG, and a steady expression strain pGEX-MUC1 / DH5 alpha is obtained through the screening. The bacteria pyrolysis is performed by boiling, the expression of MUC1-GST fusion protein is analyzed, and a specific expression band is appraised. Engineering bacteria are cultivated, a supernatant fluid is retained after the ultrasonication, and human MUC1-GST fusion protein is purified through a Glutathione-Sepharose 4B affinity layer. Then pure MUC1 polypeptide is obtained through thrombin pyrolysis and is prepared into a pharmaceutical preparation.

Description

Technical field: [0001] The invention discloses a MUC1 tandem repeat sequence polypeptide and a preparation process thereof. The invention also provides the application of the polypeptide as an antitumor drug, which belongs to the technical field of tumor treatment. Background technique: [0002] MUC1 is one of the members of the mucin family, which consists of a polypeptide backbone (core peptide) and side branch sugar chains. The polypeptide backbone of MUC1 consists of three parts: extracellular segment, transmembrane segment and intracellular segment. The extracellular segment contains a variable number of tandem repeats (variable number of tandem repeats, VNTRs), each repeat sequence contains 20 amino acids, namely SAPDTRPAPGSTAPPAHGVT. The number of VNTRs in different individuals ranged from 20-125. [0003] MUC1 is mainly distributed on the surface of epithelial cells and their derived tumor cells (breast cancer, ovarian cancer, lung cancer, pancreatic cancer, etc.)...

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): C07K7/08C07K14/47C12N15/12C12N15/70A61K38/10A61K38/17A61P35/00
Inventor 台桂香柳忠辉
Owner 台桂香
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