Molecular mechanisms of the binding, insertion, and orientation of antimicrobial peptides in model membranes

Abstract

Antimicrobial peptides (AMPs) are natural compounds widespread throughout the evolutionary scale, capable of causing the growth inhibition on pathogenic microorganisms, with potential to act controlling infections caused by multiresistant bacteria and act as natural food preservatives. The mechanism of action of many AMPs seems to depend on the balance between the physico-chemical properties of the peptide and the membrane composition of the target cell. In this project, the study of the mechanism of action of PAMs from the groups of Temporins, analogs of Plantaricin149, and peptides isolated from the skin of amphibians belonging to the family Hylidae, is proposed by means of performing multiple biophysical assays (surface tension measurements, conventional, oriented, and synchrotron radiation circular dichroism spectroscopies, and optical microscopy), employing several membrane models (micelles, lipid mono- and bilayers, large and giant vesicles) to investigate the binding, insertion, and orientation of these AMPs in these systems. Such analyses will be correlated with their respective inhibitory action in ESKAPE bacterial strains that easily escape from the action of conventional antibiotics. (AU)