Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8553369 | Toxicology Letters | 2018 | 7 Pages |
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 4.2â¯Ãâ¯104 and 4.1â¯Ãâ¯104â¯L/mol, respectively, and the lowest binding energies of BDE-47-AChE and BDE-209-AChE were â7.8 and â5.9â¯kJ/mol, respectively. BDE-47 is more likely to bind with AChE than BED-209.
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Authors
Shutao Wang, Chuan Wu, Zhisheng Liu, Hong You,