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Conformational stability and activity of circular enterocin as-48 derivatives
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نویسنده
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sańchez-hidalgo m. ,ferńandez-escamilla a.m. ,martińez-bueno m. ,valdivia e. ,serrano l. ,maqueda m.
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منبع
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protein and peptide letters - 2010 - دوره : 17 - شماره : 6 - صفحه:708 -714
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چکیده
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Four as-48 mutants (trp24ala,gly13lys,leu40lys and ala53ser) were obtained by site-directed mutagenesis. the minimal inhibitory concentration of each peptide showed that only residue trp24 was unquestionably involved in the biological activity. guanidine hydrochloride-induced unfolding assays showed a three-state transition denaturation process,suggesting a molten-globule-like conformation after the first transition. © 2010 bentham science publishers ltd.
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کلیدواژه
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Circular antimicrobial peptides; Enterococci.; Lactic-acid bacteria; Site-directed mutagenesis
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آدرس
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depto. de microbiología,facultad de ciencias, Spain, depto. de microbiología,facultad de ciencias, Spain, depto. de microbiología,facultad de ciencias, Spain, depto. de microbiología,facultad de ciencias, Spain, depto. de microbiología,facultad de ciencias, Spain
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Authors
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