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Mode of action of linear amphipathic α‐helical antimicrobial peptides

Mode of action of linear amphipathic α‐helical antimicrobial peptides 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 destruction/solubilization 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 mechanism. © 1999 John Wiley & Sons, Inc. Biopoly 47: 451–463, 1998 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biopolymers Wiley

Mode of action of linear amphipathic α‐helical antimicrobial peptides

Oren, Ziv; Shai, Yechiel
Biopolymers , Volume 47 (6) – Jan 1, 1998
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References (140)

Publisher
Wiley
Copyright
Copyright © 1998 John Wiley & Sons, Inc.
ISSN
0006-3525
eISSN
1097-0282
DOI
10.1002/(SICI)1097-0282(1998)47:6<451::AID-BIP4>3.0.CO;2-F
pmid
10333737
Publisher site
See Article on Publisher Site

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 destruction/solubilization 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 mechanism. © 1999 John Wiley & Sons, Inc. Biopoly 47: 451–463, 1998

Journal

Biopolymers – Wiley

Published: Jan 1, 1998

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