Characterization of the binding of 2‐mercaptobenzimidazole to bovine serum albumin. Issue 4 (12th February 2015)

• Record Type: Journal Article
• Authors: Teng, Yue; Zou, Luyi; Huang, Ming; Zong, Wansong
• Is Part Of: Journal of molecular recognition. Volume 28:Issue 4(2015:Apr.)
• Page Start: 232
• Page End: 238
• Publication Date: 2015-02-12
• Subjects: serum albumin -- 2‐mercaptobenzimidazole -- multi‐spectroscopic techniques -- displacement experiments -- molecular docking; Molecular recognition -- Periodicals; Models, Molecular -- Periodicals; Molecular Conformation -- Periodicals; Molecular Sequence Data -- Periodicals; Molecular Structure -- Periodicals; Carrier Proteins -- Periodicals; 572.8
• DOI: 10.1002/jmr.2437
• Languages: English
• ISSNs: 0952-3499

Abstract

Abstract : 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. Abstract : The positively charged MBI can spontaneously bind with the negatively charged BSA at site II (subdomain IIIA) through electrostatic forces with one binding site to form the MBI–BSA complex, which further led to some secondary structure and microenvironmental changes of BSA.