Differences between the binding modes of enantiomers S/R-nicotine to acetylcholinesterase.

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 (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 m

SUBMITTER: Yang J 

PROVIDER: S-EPMC9059617 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature