Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation.
Antimicrobial peptides have two binding states in a lipid bilayer, a surface state S and a pore-forming state I. The transition from the S state to the I state has a sigmoidal peptide-concentration dependence indicating cooperativity in the peptide-membrane interactions. In a previous paper, we reported the transition of alamethicin measured in three bilayer conditions. The data were explained by a free energy that took into account the membrane thinning effect induced by the peptides. In this paper, the full implications of the free energy were tested by including another type of peptide, melittin, that forms toroidal pores, instead of barrel-stave pores as in the case of alamethicin. The S-to-I transitions were measured by oriented circular dichroism. The membrane thinning effect was measured by x-ray diffraction. All data were in good agreement with the theory, indicating that the membrane thinning effect is a plausible mechanism for the peptide-induced pore formations.
Chen
Fang-Yu
FY
Department of Physics, National Central University, Chung-Li, Taiwan 32054, ROC. fychen@joule.phy.ncu.edu.tw
Lee
Ming-Tao
MT
Huang
Huey W
HW
D000408:Alamethicin / Q000737:chemistry*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D002942:Circular Dichroism; D003198:Computer Simulation; D004548:Elasticity; D008051:Lipid Bilayers / Q000737:chemistry*; D046911:Macromolecular Substances; D008555:Melitten / Q000737:chemistry*; D008560:Membrane Fluidity; D008565:Membrane Proteins / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry; D010539:Permeability; D016062:Porosity; D011485:Protein Binding; D011487:Protein Conformation; D014961:X-Ray Diffraction
D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers; D046911:Macromolecular Substances; D008565:Membrane Proteins; D010455:Peptides; D008555:Melitten; D000408:Alamethicin