Structure-activity relationships in the peptide antibiotic nisin: Antibacterial activity of fragments of nisin
Structure-activity relationships in the peptide antibiotic nisin: Antibacterial activity of fragments of nisin
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DOI：
10.1016/0014-5793(96)00638-2
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发表时间：
1996-07-22
期刊：
影响因子：
3.5
通讯作者：
Roberts, GCK
中科院分区：
文献类型：
--
作者：
Chan, WC;Leyland, M;Roberts, GCK
翻译后修饰的多肽抗生素Nisin已被一些蛋白酶切割，产生的片段经过纯化、化学表征和抑制乳酸乳球菌MG1614和黄色微球菌NCDO8166生长的活性测定。这些结果提供了关于Nisin分子不同部分对其生长抑制活性的重要性的信息，去除C末端的5个残基会导致效价降低约10倍，而去除另外9个残基(包括两个羊硫环)会导致效价降低100倍。Nisin和Subtilin的类似片段之间存在一些差异，这表明可能在作用模式上的细微差异，在羊毛硫宁环C内的裂解或去除本质上取消了Nisin的活性。片段Nisin(1-12)本身是无效的，并且特异性地拮抗Nisin的生长抑制作用。根据Nisin作用机制的现有模型对这些结果进行了讨论。
The post-translationally modified peptide antibiotic nisin has been cleaved by a number of proteases and the fragments produced purified, characterised chemically, and assayed for activity in inhibiting the growth of Lactococcus lactis MG1614 and Micrococcus luteus NCDO8166. These results provide information on the importance of different parts of the nisin molecule for its growth-inhibition activity, Removal of the C-terminal five residues leads to approximately a 10-fold decrease in potency, while removal of a further nine residues, encompassing two of the lanthionine rings, leads to a 100-fold decrease. There are some differences between analogous fragments of nisin and subtilin, suggesting possible subtle differences in mode of action, Cleavage within, or removal of, lanthionine ring C essentially abolishes the activity of nisin. The fragment nisin(1-12) is inactive itself, and specifically antagonises the growth-inhibitory action of nisin. These results are discussed in terms of current models for the mechanism of action of nisin.