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Toxicol Lett. 2018 May 1;287:42-48. doi: 10.1016/j.toxlet.2018.01.018. Epub 2018 Feb 1.

Studies on the interaction of BDE-47 and BDE-209 with acetylcholinesterase (AChE) based on the neurotoxicity through fluorescence, UV-vis spectra, and molecular docking.

Author information

1
State Key Laboratory of Urban Water Resource and Environment, Harbin Institute of Technology, Harbin, 150090, China. Electronic address: wshutao@hit.edu.cn.
2
State Key Laboratory of Urban Water Resource and Environment, Harbin Institute of Technology, Harbin, 150090, China. Electronic address: 569271730@qq.com.
3
Changchun Institute of Urban Planning & Design, Changchun, 130033, China. Electronic address: chinalzs@163.com.
4
State Key Laboratory of Urban Water Resource and Environment, Harbin Institute of Technology, Harbin, 150090, China. Electronic address: youhong@hit.edu.cn.

Abstract

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 × 104 and 4.1 × 104 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.

KEYWORDS:

Acetylcholinesterase (AChE); BDE-209; BDE-47; Molecular docking; Spectra

PMID:
29407791
DOI:
10.1016/j.toxlet.2018.01.018
[Indexed for MEDLINE]

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