Wang Shutao, Wu Chuan, Liu Zhisheng, You Hong
State Key Laboratory of Urban Water Resource and Environment, Harbin Institute of Technology, Harbin, 150090, China.
Changchun Institute of Urban Planning & Design, Changchun, 130033, China.
Toxicol Lett. 2018 May 1;287:42-48. doi: 10.1016/j.toxlet.2018.01.018. Epub 2018 Feb 1.
The neurotoxicity of polybrominated diphenyl ethers (PBDEs) has been of concern. Acetylcholinesterase (AChE) is a critical enzyme in the central and peripheral nervous system related to neurotoxicity. The interaction between BDE-47, BDE-209, and AChE was investigated through fluorescence and UV-vis spectra combined with molecular docking. Both BDE-47 and BDE-209 bound with AChE and changed the microenvironment of some amino acid residues, resulting in a change of AChE conformation. Hydrophobic interaction is the main binding force between BDE-47, BDE-209, and AChE, and electrostatic interaction exists according to the thermodynamic parameters of the interaction between them. A hydrophobic interaction of BDE-47-AChE and BDE-209-AChE has been confirmed through molecular docking to dominate the binding force. The binding constants of BDE-47-AChE and BDE-209-AChE were 4.2 × 10 and 4.1 × 10 L/mol, respectively, and the lowest binding energies of BDE-47-AChE and BDE-209-AChE were -7.8 and -5.9 kJ/mol, respectively. BDE-47 is more likely to bind with AChE than BED-209.
多溴二苯醚（PBDEs）的神经毒性一直备受关注。乙酰胆碱酯酶（AChE）是中枢和外周神经系统中与神经毒性相关的关键酶。通过荧光光谱、紫外可见光谱结合分子对接研究了BDE - 47、BDE - 209与AChE之间的相互作用。BDE - 47和BDE - 209均与AChE结合，并改变了一些氨基酸残基的微环境，导致AChE构象发生变化。疏水相互作用是BDE - 47、BDE - 209与AChE之间的主要结合力，根据它们之间相互作用的热力学参数可知还存在静电相互作用。通过分子对接证实了BDE - 47 - AChE和BDE - 209 - AChE的疏水相互作用主导了结合力。BDE - 47 - AChE和BDE - 209 - AChE的结合常数分别为4.2×10和4.1×10 L/mol，BDE - 47 - AChE和BDE - 209 - AChE的最低结合能分别为 - 7.8和 - 5.9 kJ/mol。BDE - 47比BDE - 209更易与AChE结合。
