Micelle bound structure and model membrane interaction studies of the peptide Hylin a1 from the arboreal south American frog Hypsiboas albopunctatus
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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 β-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.
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Amphipathic, Antimicrobial peptide, Frog skin secretion, Hemolytic, Hylin a1, NMR, Pore formation, Structure
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Inglês
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Protein and Peptide Letters, v. 22, n. 8, p. 719-726, 2015.
