Micelle Bound Structure and Model Membrane Interaction Studies of the Peptide Hylin a1 from the Arboreal South American Frog Hypsiboas albopunctatus

Title:Micelle Bound Structure and Model Membrane Interaction Studies of the Peptide Hylin a1 from the Arboreal South American Frog Hypsiboas albopunctatus

Volume: 22 Issue: 8

Author(s): Eliane S.F. Alves, Crusca E., Eduardo M. Cilli, Mariana S. Castro, Wagner Fontes, Mariana T. Q. de Magalhães, Luciano M. Lião and Aline L. de Oliveira

Affiliation:

Keywords: Amphipathic, antimicrobial peptide, frog skin secretion, hemolytic, Hylin a1, NMR, pore formation, structure.

Abstract: 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.

Cite this article as:

Alves S.F. Eliane, E. Crusca, Cilli M. Eduardo, Castro S. Mariana, Fontes Wagner, de Magalhães T. Q. Mariana, Lião M. Luciano and de Oliveira L. Aline, Micelle Bound Structure and Model Membrane Interaction Studies of the Peptide Hylin a1 from the Arboreal South American Frog Hypsiboas albopunctatus , Protein & Peptide Letters 2015; 22 (8) . https://dx.doi.org/10.2174/0929866522666150610092657

DOI https://dx.doi.org/10.2174/0929866522666150610092657	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305