title: Magainin 2 in phospholipid bilayers: peptide orientation and lipid chain ordering studied by X-ray diffraction.
abstract: We present a structural study of biomimetic lipid bilayers interacting with the antimicrobial peptide magainin 2 amide, using grazing incidence X-ray diffraction and reciprocal space mapping (RSM) techniques. The short-range order of lipid chains in lecithin is found to be strongly reduced by the peptides. From the scattering intensity of the chain correlation peak, we can quantify the lateral length scale R over which the bilayer structure is affected by peptide binding. The non-local perturbation of the bilayer is discussed in the framework of bilayer elasticity theory.
authors: Experimentalphysik, Universität des Saarlandes, Saarbrücken, Germany.
authors: Christian
authors: C
authors: Münster
authors: Alexander
authors: A
authors: Spaar
authors: Burkhard
authors: B
authors: Bechinger
authors: Tim
authors: T
authors: Salditt
mesh_terms: D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D054806:Magainins; D008969:Molecular Sequence Data; D010743:Phospholipids / Q000737:chemistry*; D011487:Protein Conformation; D014961:X-Ray Diffraction / Q000379:methods; D029867:Xenopus Proteins
chemical_list: D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers; D054806:Magainins; D010743:Phospholipids; D029867:Xenopus Proteins; C053301:magainin 2 peptide, Xenopus