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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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نویسنده
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alves e.s.f. ,junior e.c. ,cilli e.m. ,castro m.s. ,fontes w. ,de magalhães m.t.q. ,lião l.m. ,de oliveira a.l.
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منبع
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protein and peptide letters - 2015 - دوره : 22 - شماره : 8 - صفحه:719 -726
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چکیده
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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. © 2015 bentham science publishers.
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کلیدواژه
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Amphipathic; Antimicrobial peptide; Frog skin secretion; Hemolytic; Hylin a1; NMR; Pore formation; Structure
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آدرس
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chemistry institute,federal university of goiás, Brazil, institute of chemistry,unesp,araraquara,brazil,physics institute of são carlos,university of são paulo, Brazil, institute of chemistry,unesp, Brazil, institute of biological sciences,university of brasília, Brazil, institute of biological sciences,university of brasília, Brazil, chemistry institute,federal university of goiás,goiânia,brazil,biology institute,federal university of goiás, Brazil, chemistry institute,federal university of goiás, Brazil, chemistry institute,federal university of goiás,goiânia,brazil,chemistry institute,university of brasília,campus universitário darcy ribeiro,caixa postal 04478,asa norte,brasília, Brazil
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Authors
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