Molecular mechanism of Peptide-induced pores in membranes.
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.
Huang
Huey W
HW
Department of Physics & Astronomy, Rice University, Houston, Texas 77251, USA.
Chen
Fang-Yu
FY
Lee
Ming-Tao
MT
D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000378:metabolism*; D008051:Lipid Bilayers / Q000737:chemistry* / Q000378:metabolism*; D008954:Models, Biological; D013816:Thermodynamics
D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers