title: Characterization of the binding of 2-mercaptobenzimidazole to bovine serum albumin.
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.
authors: School of Environmental and Civil Engineering, Jiangnan University, 1800# Lihu Avenue, Wuxi, 214122, China.
authors: Yue
authors: Y
authors: Teng
authors: Luyi
authors: L
authors: Zou
authors: Ming
authors: M
authors: Huang
authors: Wansong
authors: W
authors: Zong
mesh_terms: D000818:Animals; D001562:Benzimidazoles / Q000737:chemistry* / Q000378:metabolism; D002417:Cattle; D006801:Humans; D062105:Molecular Docking Simulation; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013056:Spectrophotometry, Ultraviolet
chemical_list: D001562:Benzimidazoles; D012710:Serum Albumin, Bovine; C030698:2-mercaptobenzimidazole
keywords: 2-mercaptobenzimidazole; displacement experiments; molecular docking; multi-spectroscopic techniques; serum albumin