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Mode of action of linear amphipathic α‐helical antimicrobial peptides
Author(s) -
Oren Ziv,
Shai Yechiel
Publication year - 1998
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(1998)47:6<451::aid-bip4>3.0.co;2-f
Subject(s) - antimicrobial peptides , chemistry , antimicrobial , amphiphile , peptide , mechanism of action , mode of action , membrane , biophysics , transmembrane protein , mechanism (biology) , combinatorial chemistry , biochemistry , stereochemistry , receptor , organic chemistry , biology , in vitro , physics , quantum mechanics , copolymer , polymer
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