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环状肠球菌AS-48衍生物的构象稳定性与活性

Conformational stability and activity of circular Enterocin AS-48 derivatives.

作者信息

Sánchez-Hidalgo Marina, Fernández-Escamilla Ana M, Martínez-Bueno Manuel, Valdivia Eva, Serrano Luis, Maqueda Mercedes

机构信息

Department de Microbiología, Facultad de Ciencias, Universidad de Granada, Spain.

出版信息

Protein Pept Lett. 2010 Jun;17(6):708-14. doi: 10.2174/092986610791190390.

DOI:10.2174/092986610791190390
PMID:19958277
Abstract

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.

摘要

通过定点诱变获得了四个AS-48突变体（Trp24Ala、Gly13Lys、Leu40Lys和Ala53Ser）。每种肽的最低抑菌浓度表明，只有残基Trp24无疑参与了生物活性。盐酸胍诱导的去折叠试验显示出三态转变变性过程，表明在第一次转变后形成了类似熔球的构象。

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