Filling gaps in the knowledge of melittin on lipid membranes

TISSERA MJ; , DISALVO. E ANIBAL; F. MARTINI; CUTRO, ANDREA

COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2019 vol. 561 p. 136 - 146

0927-7757

Melittin (ML) is a small peptide of 26 residues rich in arginine (Arg) and lysine (Lys). Several studies have beendone to understand the mechanism of interaction with neutral and negatively charged lipids. However, it is notknown with certainty how this interaction depends on the electrostatic or hydrophobic forces according to thecomposition of the membrane, nor with the different organization of lipids on the membrane, such as the microdomains that could take place in it. Therefore, comparative studies of the interaction and the effect of MLwith respect to cationic peptides (Arg-7 and Lys-5) were conducted to get a deeper insight of the ML interactionmechanism with membranes. In this regard, measurements of zeta potential of different model membranes(DOPC, DMPC and DMPE liposomes) in the presence of the peptides, and molecular dynamics simulations wereperformed. In the special case of DMPC, we worked in its gel like-ripple phase, in order to analyzed defects ofpacking that potentially expose hydrocarbon regions.In relation with experimental results, molecular analysis of ML interaction with zwiterionic lipid membranein its ripple phase was performed by unbiased molecular dynamics simulations.The results allow us to remark that ML penetration is favored in the gel-liquid crystalline phase transition in