title: Peptide pores in lipid bilayers: voltage facilitation pleads for a revised model.
abstract: We address the problem of antimicrobial peptides that create pores in lipid bilayers, focusing on voltage-temperature dependence of pore opening. Two novel experiments (voltage clamp with alamethicin as an emblematic representative of these peptides and neutron reflectivity of lipid monolayer at solid-water interface under electric field) serve to revise the only current theoretical model. We introduce a general contribution of peptide adsorption and electric field as being responsible for an unbalanced tension of the two bilayer leaflets and we claim that the main entropy cost of one pore opening is due to the corresponding excluded area for lipid translation.
authors.affiliation: Laboratoire Léon Brillouin, CEA/CNRS UMR 12, CEA-Saclay, 91191 Gif-sur-Yvette, France.
authors.forename: G C
authors.initials: GC
authors.lastname: Fadda
authors.forename: D
authors.initials: D
authors.lastname: Lairez
authors.forename: Z
authors.initials: Z
authors.lastname: Guennouni
authors.forename: A
authors.initials: A
authors.lastname: Koutsioubas
mesh_terms: D015060:1,2-Dipalmitoylphosphatidylcholine / Q000737:chemistry; D000327:Adsorption; D000408:Alamethicin / Q000737:chemistry; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000378:metabolism*; D019277:Entropy; D008051:Lipid Bilayers / Q000737:chemistry* / Q000378:metabolism*; D008954:Models, Biological; D008956:Models, Chemical; D018408:Patch-Clamp Techniques
chemical_list: D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers; D015060:1,2-Dipalmitoylphosphatidylcholine; D000408:Alamethicin