期刊
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
卷 202, 期 -, 页码 1-12出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2018.04.070
关键词
Triclocarban; Bovine serum albumin; Interaction; Molecular docking; Molecular dynamics simulation
类别
资金
- National Natural Science Foundation of China [21506152]
- Natural Science Foundation of Tianjin [15JCQNJC06200]
- Beiyang Young Scholar of Tianjin University
- China Scholarship Council [201606255007]
The antimicrobial triclocarban (TCC) is frequently found in various personal care products (PCPs), and recent studies have demonstrated that it shows a high unintended biological activity on humans and wildlife. To evaluate the toxicity of TCC at the protein level, the effect of TCC on bovine serum albumin (BSA) has been investigated using various spectroscopic methods in combination with molecular modeling. Analysis of fluorescence quenching data of BSA revealed the formation of a ground state BSA-TCC complex with a binding constant of 2.58 x 10(4) M-1 at 298 K. The values of the thermodynamic parameters suggested that the binding of TCC to BSA was driven mainly by hydrophobic interaction and hydrogen bond. Site marker competitive experiments coupled with molecular docking studies confirmed that site I was the main binding site for TCC on BSA. Furthermore, TCC binding to BSA led to conformational and structural alterations of BSA as revealed by multi spectroscopic studies. In addition, the stability of BSA and BSA-TCC complex were well analyzed by the molecular dynamics studies. In short, this work indicated that TCC could interact with BSA and impact the conformation of BSA, which could provide valuable information to understand the toxicity mechanism of TCC. (C) 2018 Elsevier B.V. All rights reserved.
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