Melittin antitone analogue and preparation method for same

A melittin anti-analog technology, which is applied in the field of melittin reverse analogs and its preparation, can solve the problems of disappearance of hemolytic activity and limitation of clinical application, and achieve low immunogenicity and good water solubility , the effect of good stability

Inactive Publication Date: 2013-09-11
GUANGZHOU GLAM BIOTECH
View PDF2 Cites 9 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Melittin has a strong inhibitory effect on both Gram-positive and negative bacteria, and has a strong hemolytic activity, which limits its clinical application
Melittin has a high affinity for calmodulin. According to the model that calmodulin can bind to the polypeptide binding site, it is predicted and proved by experiments that the binding site of melittin and calmodulin is 12-26 fragments of Mel( 12~26), and found that this fragment still retains some antibacterial activity, but the hemolytic activity disappears

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
  • Melittin antitone analogue and preparation method for same
  • Melittin antitone analogue and preparation method for same

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0033] 1. Solid-phase chemical peptide synthesis reaction of reverse sequence analogue of melittin

[0034] We designed and synthesized a series of reverse peptide analogs based on Mel(12-26) with different numbers of basic amino acid residues and different chain lengths of hydrophobic fragments. Bacterial activity is very important, and the N-terminal retains at least 3 basic amino acids (positive charge > 4) and the C-terminal hydrophobic segment with a chain length of at least 8 amino acid residues has higher antibacterial activity. The hemolytic activity of sequence peptides is very small.

[0035] According to the core functional sequence of Melittin, the reverse sequence of Melittin (12-24): RKRKIWSILAPLG-COOH in the fifth position of I is replaced by R, and a basic amino acid is added to further enhance the positive charge. At the same time, the 8 hydrophobic amino acids at the C-terminal remain unchanged. The amino acid sequence is: RKRKRWSILAPLG-COOH. The N-terminal ...

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 melittin antitone analogue and a preparation method for the same. The amino acid sequence of the melittin antitone analogue is RKRKRWSILAPLG. The preparation method for the melittin antitone analogue comprises the steps of taking materials, reacting, purifying, performing mass spectrometry analysis-identification, and the like. According to the melittin antitone analogue and the preparation method for the same disclosed by the invention, the bacteriostatic activity is improved.

Description

technical field [0001] The invention relates to the field of polypeptide synthesis, in particular to a reverse sequence analog of melittin and a preparation method thereof. Background technique [0002] Antimicrobial peptides have become new drugs with important potential value due to their high efficiency, broad spectrum, rapidity, specificity, antibacterial, antiviral, antitumor and other activities and low toxicity to eukaryotic cells. Today, when traditional antibiotics are faced with increasing drug resistance of pathogenic bacteria, the emergence of antimicrobial peptides has undoubtedly become a valuable new antibacterial drug and has attracted people's attention. Maximizing its activity and reducing toxicity are the primary issues in the development of new antimicrobial peptide drugs. Modification of antimicrobial peptides by means of molecular design has become the key to solve this problem. Taking the amphiphilic α-helical antimicrobial peptide as the object, th...

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): C07K7/08C07K1/06C07K1/04
CPCY02P20/141
Inventor 李本涛印遇龙何宏轩夏新界王从峰李爱科佘锐萍李刚李帅伟
Owner GUANGZHOU GLAM BIOTECH
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