Membrane association and pore formation by alpha-helical peptides.
Membrane-active peptides exhibit antimicrobial, channel-forming and transport activities and have therefore early on been interesting targets for biophysical investigations. When the peptide-lipid interactions are studied a dynamic view emerges in which the peptides change conformation upon membrane insertion, can adopt a variety of topologies and change the macroscopic phase properties of the membrane locally or globally. Interestingly several proteins have been identified that also interact with the membrane in a dynamic fashion and where the lessons learned from peptides may add to our understanding of the ways these proteins function.
Bechinger
Burkhard
B
lnstitut de chimie, CNRS-Université de Strasbourg, UMR 7177, 4, rue Blaise Pascal, 67070 Strasbourg, France. bechinger@chimie.u-strasbg.fr
D000890:Anti-Infective Agents / Q000737:chemistry* / Q000378:metabolism; D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism; D008051:Lipid Bilayers / Q000737:chemistry* / Q000378:metabolism; D008956:Models, Chemical; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D052899:Pore Forming Cytotoxic Proteins / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary
D000890:Anti-Infective Agents; D008051:Lipid Bilayers; D010455:Peptides; D052899:Pore Forming Cytotoxic Proteins