期刊
FEBS LETTERS
卷 582, 期 21-22, 页码 3237-3242出版社
WILEY
DOI: 10.1016/j.febslet.2008.08.018
关键词
enterocin AS-48; bacteriocin; circular protein; limited proteolysis; protein fragment; antimicrobial activity
资金
- Spanish Direccion General de Investigacion Cientifica y Tecnica [BIO2005-01544]
- Grupo de Investigacion de la Junta de Andalucia [CIV 016]
- panish Ministry of Education, Culture and Sports
AS-48 is a 70-residue circular peptide from Enterococcus faecalis with a broad antibacterial activity. Here, we produced by limited proteolysis a protein species carrying a single nicking and fragments of 55 and 38 residues. Nicked AS-48 showed a lower helicity by far-ultraviolet circular dichroism and a reduced stability to thermal denaturation, but it was active against the sensitive bacteria assayed. The fragments also partly retained the biological activity of the intact protein. These results indicate that circularization is not required for the bactericidal activity, but it is important to stabilize the native structure. Moreover, it is possible to reduce the sequence to a minimal AS-48 domain without causing inactivation of this bacteriocin. (c) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据