Natural cholinesterase inhibitors from Myristica cinnamomea King

Siti Mariam Abdul Wahab, Yasodha Sivasothy, Sook Yee Liew, Marc Litaudon, Jamaludin Mohamad, Khalijah Awang

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23 Citations (Scopus)


A new acylphenol, malabaricone E (1) together with the known malabaricones A-C (2–4), maingayones A and B (5 and 6) and maingayic acid B (7) were isolated from the ethyl acetate extract of the fruits of Myristica cinnamomea King. Their structures were determined by 1D and 2D NMR techniques and LCMS-IT-TOF analysis. Compounds 3 (1.84 ± 0.19 and 1.76 ± 0.21 μM, respectively) and 4 (1.94 ± 0.27 and 2.80 ± 0.49 μM, respectively) were identified as dual inhibitors, with almost equal acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes inhibiting potentials. The Lineweaver–Burk plots of compounds 3 and 4 indicated that they were mixed-mode inhibitors. Based on the molecular docking studies, compounds 3 and 4 interacted with the peripheral anionic site (PAS), the catalytic triad and the oxyanion hole of the AChE. As for the BChE, while compound 3 interacted with the PAS, the catalytic triad and the oxyanion hole, compound 4 only interacted with the catalytic triad and the oxyanion hole.

Original languageEnglish
Pages (from-to)3785-3792
Number of pages8
JournalBioorganic and Medicinal Chemistry Letters
Issue number15
Publication statusPublished - 1 Aug 2016
Externally publishedYes


  • Acetylcholinesterase enzyme
  • Acylphenols
  • Butyrylcholinesterase enzyme
  • Dimeric acylphenols
  • Malabaricone E
  • Myristica cinnamomea King
  • Myristicaceae

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