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The activity of an antimicrobial peptide, protegrin-1, on the well-aligned lipid bilayer deposited on a thin coverglass plate was investigated by H solid-state NMR spectroscopy. Orientational distribution and molecular motion in the lipid bilayer were determined from H solid-state NMR spectrum. Reorientational motion of lipid molecules in the vacuum-dried state was found to be small but their orientational distribution was not able to be determined. As storage times were longer, the order of the alignment of lipid molecules in the lipid bilayer and percentages involved in the toroidal pore structures increased. We found that much longer time is required to get the equilibrium state of the peptide-lipid mixture under our experimental condition for investigating the action of the antimicrobial peptide like protegrin-1 on the lipid bilayers deposited on the thin coverglass plates.  :           protegrin-1    H     .          H     .                  .                       . Protegrin-1                    .

A2H solid-state NMR study on the lipid phase change in the presence of an antimicrobial peptide

A²H solid-state NMR study on the lipid phase change in the presence of an antimicrobial peptide