Eureka AIR delivers breakthrough ideas for toughest innovation challenges, trusted by R&D personnel around the world.

Polypeptide targeting human breast cancer cells and application of polypeptide

A human breast cancer cell and targeting technology, applied in the direction of application, medical preparations of non-active ingredients, peptides, etc., can solve the problems of cumbersome preparation of antibody drugs, weak penetration, poor stability, etc., and achieve non-immunogenicity , strong selectivity and small molecular weight

Active Publication Date: 2015-01-07
THE NAT CENT FOR NANOSCI & TECH NCNST OF CHINA
View PDF2 Cites 16 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0005] However, antibody drugs have disadvantages such as cumbersome preparation, poor stability, high cost, and weak penetration.

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 targeting human breast cancer cells and application of polypeptide
  • Polypeptide targeting human breast cancer cells and application of polypeptide
  • Polypeptide targeting human breast cancer cells and application of polypeptide

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0054] Embodiment 1 Construction of the polypeptide screening system of the present invention

[0055] 1. Experimental instruments and materials

[0056] N-methylmorpholine (NMM), piperidine, trifluoroacetic acid (TFA), dichloromethane (DCM), ninhydrin, vitamin C, phenol, tetramethyluronium hexafluorophosphate (HBTU), hexahydro Pyridine, triisopropylsilane (TIS), ethanedithiol (EDT), N,N dimethylformamide (DMF), anhydrous ether, resin, methanol, various Fmoc protected amino acids, peptide synthesis tubes, shaking Bed, vacuum water pump, rotary evaporator, above reagents and materials were obtained from commercial sources.

[0057] 2. Synthesis of "one bead, one object" polypeptide library

[0058] Using the Fmoc solid-phase peptide synthesis method to synthesize a peptide library, the process of screening HER2-targeted peptides is as follows: figure 1 shown. The specific method is to couple the protected amino acids to the solid phase resin one by one, and then cleave the ...

experiment example 1

[0065] Experimental Example 1 Detection of affinity between H10F and H6F polypeptides and HER2 protein by surface plasmon resonance (SPRi) method

[0066] Spot 1 mg / mL H10F and H6F peptides and 1×PBS on the chip, incubate overnight at 4°C under humid conditions, then wash with 10×PBS for 10 minutes, then with 1×PBS for 10 minutes, and finally wash with deionized water for 2 minutes. Once, 10min each time, immersed in 1×PBS containing 5% milk, incubated overnight at 4°C, then washed with 10×PBS for 10min, 1×PBS for 10min, and finally washed twice with deionized water, 10min each time , blown dry with nitrogen, and put the chip on the machine (Plexera HT surface plasmon resonance imaging system).

[0067] The mobile phase was sequentially passed through 1×PBS, 2×PBS, 1.25 μg / mL, 2.5 μg / mL, 5 μg / mL, 10 μg / mL and 20 μg / mL human HER2 purified protein, and the SPRi signal was recorded and analyzed.

[0068] Depend on figure 2 It can be seen that the SPRi signals of H10F and H6F...

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 a polypeptide targeting human breast cancer cells and application of the polypeptide. The polypeptide is as shown in the following general formula: X1LX2X3X4X5X6X7. The invention further relates to a nucleotide sequence encoding the polypeptide and an expression vector expressing the polypeptide, as well as host cells. The invention further relates to the polypeptide, a bivalent, multivalent or polypeptide conjugate formed by the polypeptide and a pharmaceutical composition formed by the targeting polypeptide and a preparation and a developing preparation capable of killing the cancer cells, as well as the application. The polypeptide provided by the invention can realize specific binding with a marker, namely a HER2 protein of the breast cancer cells, and has an obvious targeting effect and strong selectivity; furthermore, the peptide provided by the invention can be prepared by a chemical synthesis method, and has the advantages of high purity, small molecular weight, strong specificity, no immunogenicity, safety and reliability. The polypeptide can be used for preparing a targeting probe and a pharmaceutical carrier against cancers.

Description

technical field [0001] The present invention relates to the field of medicinal chemistry, in particular to a polypeptide and its application, in particular to a polypeptide targeting breast cancer and a product derived from the peptide and capable of binding to human epidermal growth factor receptor 2 protein (HER2) And the use of the above polypeptide or its derived products in the preparation of anticancer drugs or imaging preparations. Background technique [0002] HER2 is human epidermal growth factor receptor-2, a transmembrane glycoprotein with receptor tyrosine kinase (RTK) activity encoded by the ErbB2 (NCBI Genbank, Gene ID=2064) proto-oncogene, which can initiate tyrosine kinase Regulated signal transduction system. [0003] HER2 gene amplification and protein overexpression can overtransmit signals and stimulate cancer cell proliferation (Wanyi Tai, Rubi Mahato, Kun Cheng. Journal of Controlled Release 146(2010) 264-275). Studies have shown that HER2 is overexpr...

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): C07K7/06C12N15/12C12N15/63A61K47/48A61K47/42A61K49/00A61P35/00
Inventor 王子华王蔚芝胡志远
Owner THE NAT CENT FOR NANOSCI & TECH NCNST OF CHINA
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
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