ANALYSIS OF THE PERTURBATION OF PHOSPHOLIPID MODEL MEMBRANES BY A MULTIPLE ANTIGENIC PEPTIDE

A peptide construct containing 4 peptide chains corresponding to VP1(11-25) linked to a lysine core was synthesized by solid phase methodology. The surface activity and the ability of this peptide to interact with monolayers of dipalmitoylphosphatidylcholine (DPPC), phosphatidylinositol (PI) and stearylamine (SA) was studied using Langmuir-Blodgett films. Interactions between the MAP(4)-VP1 and bilayers were determined by polarization fluorescence studies. The presence of the peptide decreases the transition temperature of DPPC/DPH liposomes thus indicating the insertion of the MAP into the bilayer core. In contrast ANS-DPPC liposomes were not affected by the presence of the peptide constructs.