title: The expanding scope of antimicrobial peptide structures and their modes of action.
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.
authors.affiliation: Biochemistry Research Group, Department of Biological Sciences, University of Calgary, Calgary, Alberta, Canada, T2N 1N4.
authors.forename: Leonard T
authors.initials: LT
authors.lastname: Nguyen
authors.forename: Evan F
authors.initials: EF
authors.lastname: Haney
authors.forename: Hans J
authors.initials: HJ
authors.lastname: Vogel
mesh_terms: D000890:Anti-Infective Agents / Q000737:chemistry* / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000494:pharmacology*; D006801:Humans; D013329:Structure-Activity Relationship
chemical_list: D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides