Antimicrobial peptides (AMPs) appear as a promising therapeutic candidate against multiresistant
pathogens, because they are able to kill microorganisms and have low toxicity of resistance
cells. Hylin a1 (Hy-a1, IFGAILPLALGALKNLIK-NH2) is a peptide extracted from the skin secretion
of the frog Hypsiboas albopunctatus, which displays antimicrobial and hemolytic activities. We report
here structural studies of Hy-a1 using different techniques such as fluorescence, CD and NMR. Our
data showed that Hy-a1 acquires a well defined amphipathic α-helix when interacting with a membrane-like environment.
Furthermore, Hy-a1 presented different affinity when compared to membranes of zwitterionic or anionic lipid composition.
Finally, we proposed a molecular interaction model of this peptide with micelles.
Keywords: Amphipathic, antimicrobial peptide, frog skin secretion, hemolytic, Hylin a1, NMR, pore formation, structure.
Rights & PermissionsPrintExport