Phospholipid Fatty Acid Structure and the Activity of Membrane-Active Peptides

Abstract

visualize and characterize the interactions of two different classes of model membranolytic peptides with supported planar lipid bilayers. Our studies provided direct evidence of membrane rearrangement and peptide aggregation by a de novo cationic antimicrobial peptide designed to adopt a helical motif in bacterial membranes. We also obtained in situ evidence of specific secondary structure motifs associated with a membrane-induced fibrillization of peptides derived from haemolytic proteins obtained from sea anemone. This coupled approach provides a unique opportunity to directly link spectroscopic details associated with peptide-membrane interactions with in situ structural insights obtained on nanometer length scales.