Neutron and X-Ray reflectivity studies at solid-liquid interfaces: the interaction of a peptide with model membranes

摘要

A neutron reflectivity structural study of model biological membranes in the gel phase interacting with a 16 amino-acid peptide is presented. Membranes were prepared with the Langmuir-Schaeffer technique and measurements were done at the solid/liquid interface. Details of the structure at the interface were obtained at 1 A resolution. While with neutral lipids no specific interaction is detected, in presence of negative charges in the membrane the peptide interacts mainly with the lipid headgroups. The complementarity of neutron and synchrotron radiation measurements is mentioned.