In situ characterization of lipid A interaction with antimicrobial peptides using surface X-ray scattering.

Lipid A structure at the air-aqueous interface has been studied using pressure-area isotherm methods coupled with the surface X-ray scattering techniques of X-ray reflectivity (XR) and grazing incidence X-ray diffraction (GIXD). Lipid A monolayers were formed at the air-aqueous interface to represent the lipid moiety of the outer membrane of Gram-negative bacteria. Lipid A structure was characterized at surface pressures between 10 and 35 mN/m. Interactions of alpha-helical antimicrobial peptides LL-37, SMAP-29 and D2A22 with lipid A monolayers were subsequently studied. Although insertion into the lipid A monolayers was observed with the alpha-helical peptides, little change was seen from the X-ray data, suggesting that the lipid A hydrocarbon chains are involved in reorientation during insertion and that the hydrocarbon chains have a relatively rigid structure.