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Evidence-Based Complementary and Alternative Medicine
Volume 2016, Article ID 7481323, 7 pages
Research Article

Primary Investigation for the Mechanism of Biatractylolide from Atractylodis Macrocephalae Rhizoma as an Acetylcholinesterase Inhibitor

1Department of Pharmacy, School of Medicine, Hunan Normal University, Changsha, Hunan 410013, China
2The First Affiliated Hospital, Hunan Normal University, 61 West Jiefang Road, Changsha, Hunan 410005, China

Received 29 May 2016; Revised 9 July 2016; Accepted 13 July 2016

Academic Editor: Hyunsu Bae

Copyright © 2016 Yong-Chao Xie et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Biatractylolide was isolated from ethyl acetate extract of dried Atractylodis Macrocephalae Rhizoma root by multistep chromatographic processing. Structure of biatractylolide was confirmed by 1H-NMR and 13C-NMR. The IC50 on acetylcholinesterase (AChE) activity was 6.5458 μg/mL when the control IC50 value of huperzine A was 0.0192 μg/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 GSK3β.