School of Life Sciences, Tianjin University, Tianjin 300072, PR China.
School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, PR China.
Spectrochim Acta A Mol Biomol Spectrosc. 2018 Sep 5;202:1-12. doi: 10.1016/j.saa.2018.04.070. Epub 2018 May 9.
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 × 10 M 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.
三氯生（TCC）是一种常见的抗菌剂，广泛应用于各种个人护理产品（PCPs）中。最近的研究表明，它对人类和野生动物具有较高的非预期生物活性。为了评估 TCC 在蛋白质水平上的毒性，本研究采用多种光谱方法结合分子建模，研究了 TCC 对牛血清白蛋白（BSA）的影响。BSA 荧光猝灭数据分析表明，在 298 K 下，TCC 与 BSA 形成了基态复合物，其结合常数为 2.58×10⁵ M。热力学参数表明，TCC 与 BSA 的结合主要是由疏水相互作用和氢键驱动的。结合分子对接研究的位点标记竞争实验证实，TCC 在 BSA 上的主要结合位点是 I 型结合位点。此外，多种光谱研究表明，TCC 与 BSA 的结合导致了 BSA 的构象和结构变化。此外，通过分子动力学研究对 BSA 和 BSA-TCC 复合物的稳定性进行了很好的分析。总之，这项工作表明，TCC 可以与 BSA 相互作用，并影响 BSA 的构象，这可为理解 TCC 的毒性机制提供有价值的信息。
