We present a molecular thermodynamic treatment of interactions between lipid bilayers and antimicrobial peptides.  We formulate a global free energy model that considers the presence of individual peptides adsorbed on the surface of the bilayer, peptides inserted into the bilayer creating pore structures and peptides forming free aggregates with lipid molecules in solution. We consider the peptide-induced changes to the membrane free energy arising from hydrophobic effects, electrostatic effects, entropic effects, and chain packing effects which are dependent on the manner in which the peptide affects the membrane structure. From this free energy model we identify conditions under which surface adsorption or transmembrane pore formation would occur, the peptide to lipid ratio at which these changes are possible and the structural features of the membrane perturbation induced by the peptide.

Molecular theory of lipid bilayer structure perturbations by interacting antimicrobial peptides

243rd National Meeting (2012)

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