Journal
TOXICOLOGY LETTERS
Volume 287, Issue -, Pages 42-48Publisher
ELSEVIER IRELAND LTD
DOI: 10.1016/j.toxlet.2018.01.018
Keywords
BDE-47; BDE-209; Acetylcholinesterase (AChE); Spectra; Molecular docking
Categories
Funding
- Scientific Research Foundation for the Returned Overseas Chinese Scholars, State Education Ministry, China
- Key Laboratory of Urban Water Resource and Environment of Harbin institute of technology, China [ES201608]
- Nanqi Ren Studio, Academy of Environment & Ecology, Harbin Institute of Technology [HSCJ201709]
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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 x 10(4) and 4.1 x 10(4) 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.
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