4.5 Article

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

期刊

TOXICOLOGY LETTERS
卷 287, 期 -, 页码 42-48

出版社

ELSEVIER IRELAND LTD
DOI: 10.1016/j.toxlet.2018.01.018

关键词

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

资金

  1. Scientific Research Foundation for the Returned Overseas Chinese Scholars, State Education Ministry, China
  2. Key Laboratory of Urban Water Resource and Environment of Harbin institute of technology, China [ES201608]
  3. Nanqi Ren Studio, Academy of Environment & Ecology, Harbin Institute of Technology [HSCJ201709]

向作者/读者索取更多资源

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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