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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

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

Volume 22, Issue 8, 2015

Page: [719 - 726] Pages: 8

DOI: 10.2174/0929866522666150610092657

Price: $65

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.

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

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