Comparative study of the interaction of melittin and lysine peptides with lipid membranes

MARIA JOSE ELIAS TISSERA; DISALVO, EDGARDO ANIBAL; ANDREA C. CUTRÓ

San Miguel, Tucumán

Congreso; XLV Reunión Anual Sociedad Argentina de Biofísica; 2016

SAB

Melittin (ML) consisting of 26 amino acids arranged in -helix, rich inarginine (Arg) and lysine (Lys). The amphipathic helix penetration intothe hydrophobic interior of membranes depends on the membrane compositionand ML concentration, being involved Arg and Lys residues.However, it is not clear the role of electrostatic forces in the interactionand perturbation in the lipid bilayer. In this context the objectiveof this study was to evaluate the interactions of ML, penta andtetra peptides of Lys (same total charge of ML and similar characteristicto the C-terminal ML,respectively) through variation of potential()of phosphatidylcholine (PC), phosphatidyletanolamine (PE) andphosphatidylglyerol (PG) unilamellar vesicles. Peptides produce lessnegative values of in DMPC, DMPE and DMPC:DMPG liposomes.