Anticancer active peptide and application

A technology of anti-cancer activity and anti-cancer peptides, applied in the direction of peptides, peptide sources, anti-tumor drugs, etc., can solve the problems of weak tumor effect, high toxicity, short half-life of anti-cancer peptides, etc., and achieve strong anti-cancer activity and enhanced effect , the effect of high serum stability

Inactive Publication Date: 2018-03-06
HUNAN NORMAL UNIVERSITY
View PDF1 Cites 2 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, there are still many challenges in the development of anticancer drugs, such as: anticancer peptides have a short half-life and are easily degraded by proteases in the body. Some anticancer peptides lack selectivity and show high toxicity, and their effect on tumors is weak, especially solid 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
  • Anticancer active peptide and application
  • Anticancer active peptide and application
  • Anticancer active peptide and application

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0026] In order to reveal the anticancer effect and activity enhancement mechanism of R-lycosin-I, we detected the activity of R-lycosin-I on A549 at the cellular level and in 3D tumor spheres, and all experiments used Lycosin-I as a control. All results were statistically and analyzed. The experiments are carried out strictly according to the Institute of Standardization.

[0027] 1. Main materials and instruments

[0028] Reagents related to cell culture were purchased from Thermo Fisher Corporation, and other reagents related to cell experiments were produced by themselves. A549 and H460 cells were purchased from the Shanghai Cell Bank of the Chinese Academy of Sciences. Fluorescently labeled Lycosin-I and R-lycossin-I were both from Jill Biochemical Company. Cellometer K2, DLS, TEM, CD, fluorescence microscope are all from our laboratory. Antibody of P27 and cytochrome C was purchased from BD Company.

[0029] 2. Experimental methods and results

[0030] 2.1 Cytotoxi...

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 an anticancer active peptide and application. By virtue of an amino acid replacement strategy, K in a Lycosin-I sequence is replaced by R, E is replaced by Q, and R-Lycosin-Iis obtained. The R-lycosin-I maintains the selectivity of the Lycosin-I and improves the cell toxicity activity for solid tumor cells. The anticancer peptide is active polypeptide toxin obtained by virtue of the modification of Lycosin-I, and the anticancer peptide contains 23 amino acid residues, the molecular weight is 2928.46Da, an isoelectric point is 12.12, and the amino acid sequence is: ArgGly Trp Phe Arg Ala Met Arg Ser Ile Ala Arg Phe Ile Ala ArgGlu Arg Leu Arg Glu His Leu.

Description

technical field [0001] The invention belongs to the technical field of polypeptide drugs in biochemistry, and specifically relates to the application of an anticancer peptide obtained through amino acid substitution in a Lycosin-I sequence in antitumor drugs. Background technique [0002] Antimicrobial peptides (ACPs) have a variety of mechanisms of action, kill cancer cells quickly, are not limited to a specific target, make it difficult to produce resistance, and have low side effects and certain selectivity, which provides great opportunities for cancer treatment. A new opportunity and direction. However, there are still many challenges in the development of anticancer drugs, such as: anticancer peptides have a short half-life and are easily degraded by proteases in the body. Some anticancer peptides lack selectivity and show high toxicity, and their effect on tumors is weak, especially on solid tumor cells. Therefore, the modification and transformation of anticancer...

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): C07K14/435A61P35/00
CPCC07K14/43518
Inventor 刘中华曾佑林梁宋平张鹏马婧
Owner HUNAN NORMAL UNIVERSITY
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