title: Molecular mechanism of Peptide-induced pores in membranes.
abstract: We suggest a physical mechanism by which antimicrobial peptides spontaneously induce stable pores in membranes. Peptide binding to a lipid bilayer causes an internal stress, or internal membrane tension, that can be sufficiently strong to create pores. Like detergents, peptides have a high affinity for the rim of the pore. Binding to the rims reduces the line tension and decreases the number of peptides causing the internal membrane tension. Consequently, the pore radius is stable. The pore formation resembles a phase transition.
authors.affiliation: Department of Physics & Astronomy, Rice University, Houston, Texas 77251, USA.
authors.forename: Huey W
authors.initials: HW
authors.lastname: Huang
authors.forename: Fang-Yu
authors.initials: FY
authors.lastname: Chen
authors.forename: Ming-Tao
authors.initials: MT
authors.lastname: Lee
mesh_terms: D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000378:metabolism*; D008051:Lipid Bilayers / Q000737:chemistry* / Q000378:metabolism*; D008954:Models, Biological; D013816:Thermodynamics
chemical_list: D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers