How do channel- and pore-forming helical peptides interact with lipid membranes and how does this account for their antimicrobial activity?
Animals and plants defend themselves against pathogenic micro-organisms by the rapid mobilization of polycationic helical amphipathic peptides. Interactions with membranes induce optimal orientation and mutual structural changes, allowing for example to form transbilayer ion channels or pores whose properties are compared in this review. Physicochemical studies of peptide-lipid interactions provide attractive approaches for drug design.
Duclohier
Hervé
H
Interactions Cellulaires et Moléculaires, UMR 6026 CNRS, Université de Rennes I, Bâtiment 14, Campus de Beaulieu, France. Herve.Duclohier@univ-rennes1.fr
D000890:Anti-Infective Agents / Q000737:chemistry / Q000493:pharmacokinetics*; D015195:Drug Design; D004347:Drug Interactions; D007473:Ion Channels / Q000494:pharmacology*; D008051:Lipid Bilayers / Q000378:metabolism / Q000494:pharmacology*; D010455:Peptides / Q000493:pharmacokinetics*; D013329:Structure-Activity Relationship
D000890:Anti-Infective Agents; D007473:Ion Channels; D008051:Lipid Bilayers; D010455:Peptides