Structural aspects of the interaction of bee venom peptide melittin with phospholipids.

Abstract

AbstractIn aqueous solution, melittin structure, investigated by CD and 1H‐nmr, depends on pH and ionic composition, which also regulate the aggregation state of the peptide. When interacting with phospholipids, however, melittin exhibits a right‐handed helical conformation without any evidence of oligomeric association. The overall bilayer structure of phospholipid aqueous dispersions is also maintained in the presence of melittin, although the permeability to aqueous solutes is considerably increased. Small‐angle neutron‐diffraction analysis of oriented multilayers confirms the existence of a lamellar profile, despite the presence of the peptide throughout each bilayer and exchangeable protons almost reaching the center of the hydrophobic alkyl chains region.