Abstract

Differential Scanning Calorimetry studies of a synthetic peptide revealed the peptide decreased the temperature of the lamellar-hexagonal phase transition of cis-trans mixtures of phosphatidylethanolamine. The transition enthalpy varied significantly with lipid composition. The findings are discussed with reference to peptide saturation on the bilayer surface, bilayer thinning and peptide orientation.

Keywords: Antimicrobial peptide, amphipathic helix, DSC, LS3, phosphatidylethanolamine, phase transition, Antimicrobial, amphipathic, phase, (LSSLLSL)3, bilayer, (DSC), crystallography, DOPE, (MLVs), EDTA, TH, PE bilayers, DPOPE