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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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