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

Cyclic peptide resistant to multi-drug resistant bacteria and preparation method and application thereof

A technology of multi-drug resistant bacteria and cyclic peptides, applied in the field of cyclic peptides, can solve the problems of identifying antimicrobial peptides, difficult and other problems, and achieve the effects of broad-spectrum killing activity, strong operability, and strong bactericidal activity

Active Publication Date: 2019-07-30
CHONGQING UNIV OF TECH
View PDF4 Cites 2 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

It is difficult to identify effective antimicrobial peptides from a large number of peptide samples and predict their antibacterial activity experimentally

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
  • Cyclic peptide resistant to multi-drug resistant bacteria and preparation method and application thereof
  • Cyclic peptide resistant to multi-drug resistant bacteria and preparation method and application thereof
  • Cyclic peptide resistant to multi-drug resistant bacteria and preparation method and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0041] The synthesis of embodiment 1 antimicrobial peptide CPeptide-A:R-R-W-W-R (Arg-Arg-Trp-Trp-Arg)

[0042] Using the Fmoc solid-phase peptide synthesis method, using dichloro resin 2-CTC resin as a carrier, first synthesize a fully protected linear peptide, use a cleavage reagent to cleavage to obtain a fully protected linear peptide, and then cyclize in the liquid phase to obtain a fully protected cyclic peptide. After deprotection with trifluoroacetic acid, the primary product of cyclic peptide was obtained by ether precipitation.

[0043] The specific operation steps are:

[0044] (1) Resin activation

[0045] Weigh 1 g of resin and swell with 10 ml of DCM (dichloromethane) at room temperature for 30 min.

[0046] (2) The first amino acid is coupled to the resin

[0047] Weigh the protected amino acid Fmoc-Arg(Pbf)-OH with a total resin substitution value of 3eq and add it to the DCM solution, then add DIEA (N,N-diisopropylethylamine) with a total resin substitution ...

Embodiment 2

[0066] Example 2 Antimicrobial peptide CPeptide-B: R-R-W-W-R-F (Arg-Arg-Trp-Trp-Arg-Phe) Synthesis Reference Example 1, wherein the (4) step amino acid coupling is (Fmoc-Trp(Pbf)-OH, Fmoc-Trp(Pbf)-OH, Fmoc-Arg(Pbf)-OH, Fmoc-Phe(Pbf)-OH).

[0067] The prepared antimicrobial peptide CPeptide-B was analyzed by mass spectrometry, and the molecular weights shown in the mass spectrum were 987.90, and the theoretical value calculated from the peptide sequence was 988.167, which proved that the prepared peptide was the designed CPeptide-B.

Embodiment 3

[0068] Embodiment 3 antimicrobial peptide CPeptide-C:R-W-W-R-F (Arg-Trp-Trp-Arg-Phe) synthesis

[0069] With reference to Example 1, wherein (3) step coupling amino acid is Fmoc-Trp(Pbf)-OH, (4) coupling amino acid is successively (Fmoc-Trp(Pbf)-OH, Fmoc-Arg(Pbf)-OH, OH, Fmoc-Phe(Pbf)-OH).

[0070] The prepared antimicrobial peptide CPeptide-C was analyzed by mass spectrometry, and the molecular weights shown in the mass spectrometry were 831.80, and the theoretical value calculated from the polypeptide sequence was 831.979. It is proved that the prepared polypeptide is the designed CPeptide-C antimicrobial peptide.

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 a cyclic peptide resistant to multi-drug resistant bacteria. The cyclic peptide resistant to the multi-drug resistant bacteria is characterized in that the amino acid sequenceis any of CPeptide-A, CPeptide-B, CPeptide-C and CPeptide-D, and the antibacterial cyclic peptide is obtained through cyclization of amido bonds formed by amino groups and carboxy groups of head and tail amino acids of any of the amino acid sequence. The four novel artificially designed cationic antibacterial peptides can be synthesized by adopting an Fmoc solid-phase chemical method, the operability is strong, and the cost is low. The cationic antibacterial peptides have broad spectrum killing activity against multidrug-resistant acinetobacter baumannii, have stronger bactericidal activity than natural antimicrobial peptides, and have no toxic effect on animal and plant cells.

Description

technical field [0001] The invention relates to an anti-multidrug-resistant bacterial cyclic peptide, a preparation method and application thereof, and relates to the field of cyclic peptides. Background technique [0002] Antibiotics have been used for more than 70 years, but due to the abuse of antibiotics, many bacteria have developed resistance to antibiotics, such as vancomycin-resistant enteric bacteria, methicillin-resistant Staphylococcus aureus, ampicillin-resistant large intestine, etc. bacilli etc. The emergence of various drug-resistant bacteria and even the emergence of superbugs have made bacterial infectious diseases an urgent problem to be solved. Due to the repeated emergence of multi-drug resistant bacteria, pathogens are resistant to traditional antibiotics, and the research and development of new antibiotics The discovery process is relatively slow. Therefore, it is very necessary to develop new, efficient and safe antibacterial drugs. [0003] Antimic...

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): C07K7/64C07K1/06C07K1/04C07K1/02A61K38/12A61P31/04
CPCA61K38/00A61P31/04C07K7/64
Inventor 王远强王昱璇杨胜喜覃仁辉林治华郭海琼何清秀
Owner CHONGQING UNIV OF TECH
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