Structure of magainin and alamethicin in model membranes studied by x-ray reflectivity.
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.
Li
C
C
Institute for X-Ray Physics, University of Göttingen, Göttingen, Germany.
Salditt
T
T
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*
D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers; D054806:Magainins; D029867:Xenopus Proteins; C053301:magainin 2 peptide, Xenopus; D000408:Alamethicin