Lys17 in the 'lasso' peptide lariatin A is responsible for anti-mycobacterial activity
Lys17 in the 'lasso' peptide lariatin A is responsible for anti-mycobacterial activity
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DOI：
10.1016/j.bmcl.2009.03.033
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发表时间：
2009-05-15
影响因子：
2.7
通讯作者：
Omura, Satoshi
中科院分区：
文献类型：
--
作者：
Iwatsuki, Masato;Koizumi, Yukio;Omura, Satoshi
用羧肽酶P水解抗分枝杆菌肽lariatin A的C-末端缺失片段，并评价其抗分枝杆菌活性。发现Lys 17对于它们的抗微生物活性是必不可少的。分子动力学模拟，明确的水分子，有助于确定Lys 17的结构特征lariatin A。模拟揭示了Lys 17的N-xi原子和C-末端Pro 18的羧基之间的盐桥的动态形成和变形，这被认为是该化合物的抗分枝杆菌活性的关键。(C)2009爱思唯尔有限公司保留所有权利。
C-terminal-lacking fragments of the anti-mycobacterial peptide lariatin A were obtained by hydrolysis using carboxypeptidase P and their anti-mycobacterial activities were evaluated. Lys17 was found to be essential for their antimicrobial activity. A molecular dynamics simulation, with explicit water molecules, helped determine the structural characteristics of Lys17 of lariatin A. The simulation revealed the dynamic formation and deformation of a salt bridge between the N-xi atom of Lys17 and the carboxyl group of C-terminal Pro18, which is deemed to be crucial for the compound's anti-mycobacterial activity. (C) 2009 Elsevier Ltd. All rights reserved.