Characterization of the binding of 2‐mercaptobenzimidazole to bovine serum albumin
Characterization of the binding of 2‐mercaptobenzimidazole to bovine serum albumin
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DOI：
10.1002/jmr.2437
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发表时间：
2015-04
影响因子：
2.7
通讯作者：
Y. Teng;Luyi Zou;Ming-Ju Huang;Wansong Zong
中科院分区：
文献类型：
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作者：
Y. Teng;Luyi Zou;Ming-Ju Huang;Wansong Zong
2-巯基苯并咪唑(MBI)被广泛用作缓蚀剂、镀铜光亮剂和橡胶促进剂。MBI在环境中的残留对人类健康具有潜在的危害。本文采用光谱和分子对接的方法，研究了生理条件下MBI与牛血清白蛋白(BSA)的相互作用。带正电荷的MBI与带负电荷的BSA可以通过一个结合位点的静电力自发结合。位点标记竞争实验和分子对接研究表明，MBI结合到BSA的II位(亚区IIIA)，进而导致BSA的一些二级结构和微环境发生变化。这项工作为在分子水平上理解MBI的毒理作用提供了有用的信息。版权所有©2015 John Wiley&Sons，Ltd.
2‐Mercaptobenzimidazole (MBI) is widely utilized as a corrosion inhibitor, copper‐plating brightener and rubber accelerator. The residue of MBI in the environment is potentially harmful to human health. In this article, the interaction of MBI with bovine serum albumin (BSA) was explored using spectroscopic and molecular docking methods under physiological conditions. The positively charged MBI can spontaneously bind with the negatively charged BSA through electrostatic forces with one binding site. The site marker competition experiments and the molecular docking study revealed that MBI bound into site II (subdomain IIIA) of BSA, which further led to some secondary structure and microenvironmental changes of BSA. This work provides useful information on understanding the toxicological actions of MBI at the molecular level. Copyright © 2015 John Wiley & Sons, Ltd.