Acetylcholinesterase inhibitory activity from growing in Chile: enzymatic and molecular docking studies.

Alkaloid profiles from plants collected in Chile were examined by GC-MS to assess their inhibitory activity on acetylcholinesterase (AChE) using and methodologies. The alkaloid extract was roughly separated by column chromatography on silica gel. AChE inhibitory activities from extracts and purified alkaloids were tested by the Ellman method and a molecular docking study was performed to assess the interaction between AChE and purified alkaloids. Sixteen alkaloids were found from hexane and chloroform extracts, and three were isolated and identified as buphanidrine, acetylcaranine and lycorine. Chloroform extract showed the greatest AChE inhibitory activity with IC value 8.89 µg/mL, whereas buphanidrine exhibited the highest inhibitory activity, with IC value 17.56 µg/mL. Inhibition kinetics showed that buphanidrine acts as a mixed inhibitor and molecular docking supports this inhibition mechanism. Overall, our study supports the potential use of as an alkaloid source with AChE inhibitory activity.[Formula: see text].