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Magainin 2 in phospholipid bilayers: peptide orientation and lipid chain ordering studied by X-ray diffraction

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Biomembranes
0005-2736
Publisher
Elsevier
Publication Date
Volume
1562
Identifiers
DOI: 10.1016/s0005-2736(02)00357-7
Keywords
  • X-Ray Diffraction
  • Antibiotic Peptide
  • Lipid–Peptide Interaction

Abstract

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.

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