Interaction of Cationic Antimicrobial Peptides with Model Membranes

Lijuan Zhang, Annett Rozek, Robert E.W. Hancock

Research output: Contribution to journalArticlepeer-review

363 Citations (Scopus)


A series of natural and synthetic cationic antimicrobial peptides from various structural classes, including α-helical, β-sheet, extended, and cyclic, were examined for their ability to interact with model membranes, assessing penetration of phospholipid monolayers and induction of lipid flip-flop, membrane leakiness, and peptide translocation across the bilayer of large unilamellar liposomes, at a range of peptide/lipid ratios. All peptides were able to penetrate into monolayers made with negatively charged phospholipids, but only two interacted weakly with neutral lipids. Peptide-mediated lipid flip-flop generally occurred at peptide concentrations that were 3- to 5-fold lower than those causing leakage of calcein across the membrane, regardless of peptide structure. With the exception of two α-helical peptides V681n and V25p, the extent of peptide-induced calcein release from large unilamellar liposomes was generally low at peptide/lipid molar ratios below 1:50. Peptide translocation across bilayers was found to be higher for the β-sheet peptide polyphemusin, intermediate for α-helical peptides, and low for extended peptides. Overall, whereas all studied cationic antimicrobial peptides interacted with membranes, they were quite heterogeneous in their impact on these membranes.

Original languageEnglish
Pages (from-to)35714-35722
Number of pages9
JournalJournal of Biological Chemistry
Issue number38
Publication statusPublished or Issued - 21 Sept 2001
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this