The expanding scope of antimicrobial peptide structures and their modes of action.

Leonard T Nguyen, Evan F Haney, Hans J Vogel

Journal: Trends in biotechnology 2011;29(9):464-72

PMID: 21680034

Abstract

Antimicrobial peptides (AMPs) are an integral part of the innate immune system that protect a host from invading pathogenic bacteria. To help overcome the problem of antimicrobial resistance, cationic AMPs are currently being considered as potential alternatives for antibiotics. Although extremely variable in length, amino acid composition and secondary structure, all peptides can adopt a distinct membrane-bound amphipathic conformation. Recent studies demonstrate that they achieve their antimicrobial activity by disrupting various key cellular processes. Some peptides can even use multiple mechanisms. Moreover, several intact proteins or protein fragments are now being shown to have inherent antimicrobial activity. A better understanding of the structure-activity relationships of AMPs is required to facilitate the rational design of novel antimicrobial agents.

Copyright © 2011 Elsevier Ltd. All rights reserved.

Address: Biochemistry Research Group, Department of Biological Sciences, University of Calgary, Calgary, Alberta, Canada, T2N 1N4.
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