Detergent-like actions of linear amphipathic cationic antimicrobial peptides.
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, delta-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.
Bechinger
Burkhard
B
Université Louis Pasteur/CNRS LC3-UMR7177, Institut/Faculté de Chimie, 4, rue Blaise Pascal, F-67070 Strasbourg, France. bechinger@chimie.u-strasbg.fr <bechinger@chimie.u-strasbg.fr>
Lohner
Karl
K
D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000494:pharmacology*; D003902:Detergents / Q000737:chemistry / Q000494:pharmacology*; D008956:Models, Chemical
D023181:Antimicrobial Cationic Peptides; D003902:Detergents