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Biophys. J. BioFAST: First Published August 18, 2006. doi:10.1529/biophysj.106.090118
© 2006 by the Biophysical Society.

A more recent version of this article appeared on November 1, 2006.
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MEMBRANES

Structure of magainin and alamethicin in model membranes studied by x-ray reflectivity

Chenghao Li 1 and Tim Salditt 2*

1 Max Planck Institute KG Golm
2 Universität Göttingen

* To whom correspondence should be addressed. E-mail: tsaldit{at}gwdg.de.

Submitted on May 30, 2006
Revised on June 29, 2006
Accepted on 14 July 2006


  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 modelling the bilayer density profile p(z). Model simulations of the reflectivity curves cover a large range of vertical momentum transfer qz, and yield excellent agreement between data and theory. The structural changes observed as a function of the molar peptide-to-lipid concentration P/L are discussed in a comparative way.

Key Words: alamethicin, antibiotic peptides, lipid membranes, magainin, x-ray reflectivity






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Copyright © 2006 by the Biophysical Society.