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Int. J. Mol. Sci. 2016, 17(8), 1330; doi:10.3390/ijms17081330

Molecular Insights into the Potential Toxicological Interaction of 2-Mercaptothiazoline with the Antioxidant Enzyme—Catalase

1
School of Environment and Civil Engineering, Jiangnan University, Wuxi 214122, China
2
Jiangsu Key Laboratory of Anaerobic Biotechnology, Jiangnan University, Wuxi 214122, China
3
Jiangsu Collaborative Innovation Center of Technology and Material of Water Treatment, Suzhou 215009, China
*
Author to whom correspondence should be addressed.
Academic Editor: Stephen C. Bondy
Received: 6 July 2016 / Revised: 2 August 2016 / Accepted: 5 August 2016 / Published: 16 August 2016
(This article belongs to the Section Molecular Toxicology)
View Full-Text   |   Download PDF [4084 KB, uploaded 16 August 2016]   |  

Abstract

2-mercaptothiazoline (2-MT) is widely used in many industrial fields, but its residue is potentially harmful to the environment. In this study, to evaluate the biological toxicity of 2-MT at protein level, the interaction between 2-MT and the pivotal antioxidant enzyme—catalase (CAT) was investigated using multiple spectroscopic techniques and molecular modeling. The results indicated that the CAT fluorescence quenching caused by 2-MT should be dominated by a static quenching mechanism through formation of a 2-MT/CAT complex. Furthermore, the identifications of the binding constant, binding forces, and the number of binding sites demonstrated that 2-MT could spontaneously interact with CAT at one binding site mainly via Van der Waals’ forces and hydrogen bonding. Based on the molecular docking simulation and conformation dynamic characterization, it was found that 2-MT could bind into the junctional region of CAT subdomains and that the binding site was close to enzyme active sites, which induced secondary structural and micro-environmental changes in CAT. The experiments on 2-MT toxicity verified that 2-MT significantly inhibited CAT activity via its molecular interaction, where 2-MT concentration and exposure time both affected the inhibitory action. Therefore, the present investigation provides useful information for understanding the toxicological mechanism of 2-MT at the molecular level. View Full-Text
Keywords: 2-mercaptothiazoline; catalase; spectroscopic technique; molecular docking; toxicity; protein conformation 2-mercaptothiazoline; catalase; spectroscopic technique; molecular docking; toxicity; protein conformation
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Huang, Z.; Huang, M.; Mi, C.; Wang, T.; Chen, D.; Teng, Y. Molecular Insights into the Potential Toxicological Interaction of 2-Mercaptothiazoline with the Antioxidant Enzyme—Catalase. Int. J. Mol. Sci. 2016, 17, 1330.

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