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 dipalmitoylphos-phatidylcholine (DPPC), phosphatidylinositol (PI) and stearylamine (SA) was studied using Langmuir-Blodgett films. Interactions between the MAP4-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.