Alpha-helical cationic antimicrobial peptides: relationships of structure and function.
10.1007/s13238-010-0004-3
- Author:
Yibing HUANG
1
;
Jinfeng HUANG
;
Yuxin CHEN
Author Information
1. Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun 130021, China.
- Publication Type:Journal Article
- MeSH:
Anti-Bacterial Agents;
chemistry;
pharmacology;
Anti-Infective Agents;
chemistry;
pharmacology;
Antimicrobial Cationic Peptides;
chemistry;
pharmacology;
Bacteria;
drug effects;
Circular Dichroism;
Drug Resistance, Microbial;
physiology;
Protein Structure, Secondary;
Structure-Activity Relationship
- From:
Protein & Cell
2010;1(2):143-152
- CountryChina
- Language:English
-
Abstract:
Antimicrobial peptides (AMPs), with their extraordinary properties, such as broad-spectrum activity, rapid action and difficult development of resistance, have become promising molecules as new antibiotics. Despite their various mechanisms of action, the interaction of AMPs with the bacterial cell membrane is the key step for their mode of action. Moreover, it is generally accepted that the membrane is the primary target of most AMPs, and the interaction between AMPs and eukaryotic cell membranes (causing toxicity to host cells) limits their clinical application. Therefore, researchers are engaged in reforming or de novo designing AMPs as a 'single-edged sword' that contains high antimicrobial activity yet low cytotoxicity against eukaryotic cells. To improve the antimicrobial activity of AMPs, the relationship between the structure and function of AMPs has been rigorously pursued. In this review, we focus on the current knowledge of α-helical cationic antimicrobial peptides, one of the most common types of AMPs in nature.
