biostudies-literatureYang JChina Tobacco Yunnan Industrial Corp1428-1440https://www.ebi.ac.uk/biostudies/studies/S-EPMC9059617biostudies-literatureUnknown9(3)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 (S/R-nicotine). Fluorescence spectroscopy showed that the quenching mechanism of endogenous fluorescence of AChE by S/R-nicotine was static, as confirmed by the time-resolved steady-state fluorescence. The binding strength of both nicotine to AChE was weak (S-AChE: K a = 80.06 L mol-1, R-AChE: K a = 173.75 L mol-1). The mRSC advancesDifferences between the binding modes of enantiomers S/R-nicotine to acetylcholinesterase.PMC90596172018CP07Tang JLi HYang JLiu ZYang LGan NChen YMiao MfalseDifferences between the binding modes of enantiomers S/R-nicotine to acetylcholinesterase.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 (S/R-nicotine). Fluorescence spectroscopy showed that the quenching mechanism of endogenous fluorescence of AChE by S/R-nicotine was static, as confirmed by the time-resolved steady-state fluorescence. The binding strength of both nicotine to AChE was weak (S-AChE: K a = 80.06 L mol-1, R-AChE: K a = 173.75 L mol-1). The m2019-01-01T00:00:00Z2019 Jan2025-04-04T08:01:24.446Z2025-04-04T08:01:24.446ZS-EPMC90596173551803110.1039/c8ra09963d