2-Mercaptothiazoline (MTZ) is broadly present in daily use as an antifungal reagent, a brightening agent, and a corrosion inhibitor. MTZ is potentially harmful for human health. Although the toxic effects of MTZ on experimental animals have been reported, the effects of MTZ on the proteins in the circulatory system at the molecular level have not been identified previously. Here, we explored the interaction of MTZ with bovine hemoglobin (BHb) in vitro using multiple spectroscopic techniques and molecular docking. In this study, the binding capacity, acting force, binding sites, molecular docking simulation, and conformational changes were investigated. MTZ quenched the intrinsic emission of BHb via the static quenching process and could spontaneously bind with BHb mainly through van der Waals forces and hydrogen bond. The computational docking visualized that MTZ bound to the β2 subunit of BHb, which further led to some changes of the skeleton and secondary structure of BHb. This research provides valuable information about the molecular mechanisms on BHb induced by MTZ and is beneficial for clarifying the toxicological actions of MTZ in blood.
Keywords: 2-Mercaptothioazoline; Binding interaction; Conformation investigation; Hemoglobin; Molecular modeling; Spectroscopic studies.