{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yang J"],"funding":["China Tobacco Yunnan Industrial Corp"],"pagination":["1428-1440"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9059617"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(3)"],"pubmed_abstract":["Nicotine causes neurotoxic effects because it quickly penetrates the blood-brain barrier after entering the human body. Acetylcholinesterase (AChE) is a key enzyme in the central and peripheral nervous system associated with neurotoxicity. In this study, a spectroscopic method and computer simulation were applied to explore the mode of interaction between AChE and enantiomers of nicotine (<i>S</i>/<i>R</i>-nicotine). Fluorescence spectroscopy showed that the quenching mechanism of endogenous fluorescence of AChE by <i>S</i>/<i>R</i>-nicotine was static, as confirmed by the time-resolved steady-state fluorescence. The binding strength of both nicotine to AChE was weak (S-AChE: <i>K</i> <sub>a</sub> = 80.06 L mol<sup>-1</sup>, R-AChE: <i>K</i> <sub>a</sub> = 173.75 L mol<sup>-1</sup>). The m"],"journal":["RSC advances"],"pubmed_title":["Differences between the binding modes of enantiomers <i>S</i>/<i>R</i>-nicotine to acetylcholinesterase."],"pmcid":["PMC9059617"],"funding_grant_id":["2018CP07"],"pubmed_authors":["Tang J","Li H","Yang J","Liu Z","Yang L","Gan N","Chen Y","Miao M"],"additional_accession":[]},"is_claimable":false,"name":"Differences between the binding modes of enantiomers <i>S</i>/<i>R</i>-nicotine to acetylcholinesterase.","description":"Nicotine causes neurotoxic effects because it quickly penetrates the blood-brain barrier after entering the human body. Acetylcholinesterase (AChE) is a key enzyme in the central and peripheral nervous system associated with neurotoxicity. In this study, a spectroscopic method and computer simulation were applied to explore the mode of interaction between AChE and enantiomers of nicotine (<i>S</i>/<i>R</i>-nicotine). Fluorescence spectroscopy showed that the quenching mechanism of endogenous fluorescence of AChE by <i>S</i>/<i>R</i>-nicotine was static, as confirmed by the time-resolved steady-state fluorescence. The binding strength of both nicotine to AChE was weak (S-AChE: <i>K</i> <sub>a</sub> = 80.06 L mol<sup>-1</sup>, R-AChE: <i>K</i> <sub>a</sub> = 173.75 L mol<sup>-1</sup>). The m","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Jan","modification":"2025-04-04T08:01:24.446Z","creation":"2025-04-04T08:01:24.446Z"},"accession":"S-EPMC9059617","cross_references":{"pubmed":["35518031"],"doi":["10.1039/c8ra09963d"]}}