Detergent-like actions of linear amphipathic cationic antimicrobial peptides

386Citations
Citations of this article
230Readers
Mendeley users who have this article in their library.

Abstract

Antimicrobial peptides have raised much interest as pathogens become resistant against conventional antibiotics. We review biophysical studies that have been performed to better understand the interactions of linear amphipathic cationic peptides such as magainins, cecropins, dermaseptin, δ-lysin or melittin. The amphipathic character of these peptides and their interactions with membranes resemble the properties of detergent molecules and analogies between membrane-active peptide and detergents are presented. Several models have been suggested to explain the pore-forming, membrane-lytic and antibiotic activities of these peptides. Here we suggest that these might be 'special cases' within complicated phase diagrams describing the morphological plasticity of peptide/lipid supramolecular assemblies. © 2006 Elsevier B.V. All rights reserved.

Cite

CITATION STYLE

APA

Bechinger, B., & Lohner, K. (2006, September). Detergent-like actions of linear amphipathic cationic antimicrobial peptides. Biochimica et Biophysica Acta - Biomembranes. https://doi.org/10.1016/j.bbamem.2006.07.001

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free