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Biatractylolide was isolated from ethyl acetate extract of dried  Atractylodis Macrocephalae Rhizoma  root by multistep chromatographic processing. Structure of biatractylolide was confirmed by  1 H-NMR and  13 C-NMR. The IC 50  on acetylcholinesterase (AChE) activity was 6.5458  μ g/mL when the control IC 50  value of huperzine A was 0.0192  μ g/mL. Molecular Docking Software (MOE) was used to discover molecular sites of action between biatractylolide and AChE protein by regular molecular docking approaches. Moreover, biatractylolide downregulated the expression of AChE of MEF and 293T cells in a dose-dependent manner. These results demonstrated that the molecular mechanisms of inhibitory activities of biatractylolide on AChE are not only through binding to AChE, but also via reducing AChE expression by inhibiting the activity of GSK3 β .

Primary Investigation for the Mechanism of Biatractylolide fromAtractylodis Macrocephalae Rhizomaas an Acetylcholinesterase Inhibitor