Interaction of alamethicin with lecithin bilayers: a 31P and 2H NMR study.

The interaction of alamethicin with artificial lecithin multilamellar dispersions was investigated by nuclear magnetic resonance (NMR) and Raman spectroscopies. 31P NMR studies revealed perturbation of the lipid head groups in the presence of the icosapeptide. Simulation of the 31P NMR spectra indicated that the observed spectral changes could be attributed to slight variations in the average tilt angle of the head groups. In contrast, no noticeable effect of the peptide on the segmental order of the hydrophobic acyl chains of the lipid molecules was detected by 2H NMR and Raman spectroscopic measurements. Taken together, these results indicated that, in the absence of a transmembrane electric potential, alamethicin interacts primarily at the water-lipid interface without significant insertion or incorporation into the bilayer leaflet.