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

Anti-tumor polypeptide targeting PKM2 protein and application of anti-tumor polypeptide

An anti-tumor and protein technology, applied in the biological field, can solve the problems of poor water solubility and limited affinity of the target protein, and achieve the effect of large sample content, abundant quantity and variety, and overcoming cumbersome steps.

Active Publication Date: 2021-03-12
SUN YAT SEN UNIV SHENZHEN
View PDF2 Cites 4 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0005] In order to overcome the shortcomings of existing PKM2 non-polypeptide organic synthetic small molecule drugs such as poor water solubility and limited affinity with target proteins, the purpose of the first aspect of the present invention is to provide an anti-tumor polypeptide targeting PKM2 protein

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
  • Anti-tumor polypeptide targeting PKM2 protein and application of anti-tumor polypeptide
  • Anti-tumor polypeptide targeting PKM2 protein and application of anti-tumor polypeptide
  • Anti-tumor polypeptide targeting PKM2 protein and application of anti-tumor polypeptide

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0047] Example 1 Screening of anti-tumor polypeptides targeting a PKM2 protein

[0048] (1) Synthesis of phosphorylated tyrosine polypeptide library

[0049] The structural formula of phosphorylated tyrosine polypeptide compound is synthesized by the synthesis of Titan 357 (AAPPTEC) synthesizers Titan 357 (AAPPTEC), and the structural form of phosphorylated tyrosine polypeptide library is: AA 5 AA 4 -py-aa 2 AA 1 -PEG-R (AA represents any type of L-type natural amino acid). The phosphorylated tyrosine polypeptide is synthesized on the Tentagel S-NH2 resin by a method of tentagel s-NH2 resin by a method of tentagel S-NH2 resin.

[0050] First, a certain amount of resin is placed in a polymerizing container (CV) swells 2 h with N-methylpyrrolidone (NMP) solution, and then adds 1 degree amount of FMOC-amino acid (FMOC-MET), 2 times equivalent O - Benzotriazole-N, N, N ', N' - tetramethylurea tetrafluororate (TBTU), 5 times the amount of diisopropylidelamine (Diea), reaction for 30min...

Embodiment 2

[0066] A kit for diagnosing tumors, including Kg-Py-Eq, Kg-PY-IW, HW-PY-KW, NK-PY-GE, RD-PY-LY, HV-PY-SR, PE-PY-YR At least one of DE-PY-FQ; the tumor is at least one of liver cancer and breast cancer.

[0067] A drug for treating tumors comprising Kg-Py-Eq, Kg-PY-IW, HW-PY-KW, NK-PY-GE, RD-PY-LY, HV-PY-SR, PE-PY-YR, At least one of DE-PY-FQ; at least one of the tumors is liver cancer, breast cancer; the drug further comprises a pharmaceutically acceptable excipient.

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 anti-tumor polypeptide targeting PKM2 protein and application of the anti-tumor polypeptide. The amino acid sequence of the polypeptide is at least one of KG-pY-EQ, KG-pY-IW, HW-pY-KW, NK-pY-GE, RD-pY-LY, HV-pY-SR, PE-pY-YR and DE-pY-FQ, wherein pY represents phosphorylated tyrosine. The anti-tumor polypeptide targeting the PKM2 protein has an inhibiting effect on growthand proliferation of liver cancer cells and breast cancer cells, and can be used for treating tumors.

Description

Technical field [0001] The present invention belongs to the biotechnology field, and more particularly to anti-tumor polypeptides targeting PKM2 proteins and their applications. Background technique [0002] Malignant tumors (cancer) have become one of the main public health issues that have seriously threatened human health, and developed a more high-efficiency drug for the diagnosis and treatment of tumors to become an important task of medical researchers. Protein kinase is considered to be an important target group of anticancer drugs in humans, protein kinases are closely involved in various life activities such as intracellular signal transduction and energy exchange, and play an essential role in maintaining cellular function and human metabolism. [0003] Unlike normal cells, the energy metabolism of cancer cells is an oxygen-sugar yeast. This low-capacity metabolic manifestation makes cancer cells as high-level glucose intake, and the intermediate product of glycolysis i...

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): C07K7/06G01N33/574A61K38/08A61P35/00
CPCC07K7/06G01N33/574A61P35/00A61K38/00
Inventor 高理钱谢刘幸谈思佳王璇李孟础杨芬贾艳肖奇才沈君
Owner SUN YAT SEN UNIV SHENZHEN
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