Structural highlights
Publication Abstract from PubMed
Antimicrobial peptides (AMPs) appear as a promising therapeutic candidate against multi-resistant 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 alpha-helix when interacting with a membrane-like environment. Furthermore, Hy-a1 presented different affinity when compared to membranes of zwitter ionic or anionic lipid composition. Finally, we proposed a molecular interaction model of this peptide with micelles.
Micelle Bound Structure and Model Membrane Interaction Studies of the Peptide Hylin a1 from the Arboreal South American Frog Hypsiboas albopunctatus.,Fernandes Alves ES, Junior EC, Cilli EM, Castro MS, Fontes W, de Magalhaes MT, Liao LM, de Oliveira AL Protein Pept Lett. 2015 Jun 9. PMID:26059694[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fernandes Alves ES, Junior EC, Cilli EM, Castro MS, Fontes W, de Magalhaes MT, Liao LM, de Oliveira AL. Micelle Bound Structure and Model Membrane Interaction Studies of the Peptide Hylin a1 from the Arboreal South American Frog Hypsiboas albopunctatus. Protein Pept Lett. 2015 Jun 9. PMID:26059694
