Mode of action of linear amphipathic α-helical antimicrobial peptides

Ziv Oren, Yechiel Shai

Research output: Contribution to journalArticlepeer-review

799 Scopus citations

Abstract

The increasing resistance of bacteria to conventional antibiotics resulted in a strong effort to develop antimicrobial compounds with new mechanisms of action. Antimicrobial peptides seem to be a promising solution to this problem. Many studies aimed at understanding their mode of action were described in the past few years. The most studied group includes the linear, mostly α-helical peptides. Although the exact mechanism by which they kill bacteria is not clearly understood, it has been shown that peptide-lipid interactions leading to membrane permeation play a role in their activity. Membrane permeation by amphipathic α-helical peptides can proceed via either one of the two mechanisms: (a) transmembrane pore formation via a "barrel-stave" mechanism; and (b) membrane destrucnonSsolubilization via a "carpet-like" mechanism. The purpose of this review is to summarize recent studies aimed at understanding the mode of action of linear α-helical antimicrobial peptides. This review, which is focused on magainins, cecropins, and dermaseptins as representatives of the amphipathic α-helical antimicrobial peptides. supports the carpet-like rather the barrel-stave mechanism. That these peptides vary with regard to their length, amino acid composition, and net positive charge, but act via a common mechanism, may imply that other linear antimicrobial peptides that share the same properties also share the same mechanisms.

Original languageEnglish
Pages (from-to)451-463
Number of pages13
JournalBiopolymers
Volume47
Issue number6
DOIs
StatePublished - 1998
Externally publishedYes

Keywords

  • Antibiotics
  • Bacteria
  • Linear amphipathic α-helical antimicrobial peptides
  • Membrane permeation
  • Peptide-lipid interactions

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