Structure, function and molecular design strategies of antibacterial peptide SMAP-29: a review.
- Author:
Chen CHEN
1
;
Sanqiao WU
;
Xinsheng LI
;
Xiaoying ZHANG
;
Maocang YAN
Author Information
1. Shaanxi Key Laboratory of Resource Biology, Shaanxi University of Technology, Hanzhong 723000, China. cchen2008@yahoo.com
- Publication Type:Journal Article
- MeSH:
Animals;
Antimicrobial Cationic Peptides;
chemistry;
genetics;
physiology;
Blood Proteins;
chemistry;
genetics;
physiology;
Cathelicidins;
chemistry;
genetics;
physiology;
Drug Design;
Recombinant Proteins;
chemistry;
genetics;
Sheep
- From:
Chinese Journal of Biotechnology
2011;27(6):846-859
- CountryChina
- Language:Chinese
-
Abstract:
Antibacterial peptides are a family of host-defense peptides most of which are gene-encoded and produced by living organisms of all types. Antibacterial peptides are small molecular proteins with broad antimicrobial spectrum against bacteria, viruses, fungi and sometimes even as anticancer peptide. SMAP-29, a cathelicidin-like peptide derived from sheep myeloid, line alpha-helical Structure, exerts a powerful broad antimicrobial activity against different pathogens including Gram-positive and Gram-negative bacteria, fungi, viruses, parasites, spirochaetes, chlamydia and antiendotoxin activity, and particular antibacterial mechanism, rapidly to permeabilize membranes of susceptible organisms. This paper summarizes the lately research progress of SMAP-29 and Variants including the characteristics of structure, structure-activity relationships, mode of action, diverse biological functions, gene recombinant and expression. We put emphasis on the necessity of molecular design, and primary and secondary structure-based modification, to provides a strong foundation for further drug development and design of SMAP-29.
