title: Structure of magainin and alamethicin in model membranes studied by x-ray reflectivity.
abstract: We have investigated the structure of lipid bilayers containing varied molar ratios of different lipids and the antimicrobial peptides magainin and alamethicin. For this structural study, we have used x-ray reflectivity on highly aligned solid-supported multilamellar lipid membranes. The reflectivity curves have been analyzed by semi-kinematical reflectivity theory modeling the bilayer density profile rho(z). Model simulations of the reflectivity curves cover a large range of vertical momentum transfer q(z), and yield excellent agreement between data and theory. The structural changes observed as a function of the molar peptide/lipid concentration P/L are discussed in a comparative way.
authors.affiliation: Institute for X-Ray Physics, University of Göttingen, Göttingen, Germany.
authors.forename: C
authors.initials: C
authors.lastname: Li
authors.forename: T
authors.initials: T
authors.lastname: Salditt
mesh_terms: D000408:Alamethicin / Q000737:chemistry*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D003198:Computer Simulation; D008051:Lipid Bilayers / Q000737:chemistry*; D054806:Magainins; D008560:Membrane Fluidity; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D014961:X-Ray Diffraction / Q000379:methods; D029867:Xenopus Proteins / Q000737:chemistry*
chemical_list: D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers; D054806:Magainins; D029867:Xenopus Proteins; C053301:magainin 2 peptide, Xenopus; D000408:Alamethicin