Natural cholinesterase inhibitors from Myristica cinnamomea King

Wahab, S.M.A. and Sivasothy, Y. and Liew, Sook Yee and Litaudon, M. and Mohamad, Jamaludin and Awang, Khalijah (2016) Natural cholinesterase inhibitors from Myristica cinnamomea King. Bioorganic & Medicinal Chemistry Letters, 26 (15). pp. 3785-3792. ISSN 0960-894X

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Official URL: http://dx.doi.org/10.1016/j.bmcl.2016.05.046

Abstract

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.

Item Type: Article
Uncontrolled Keywords: Myristica cinnamomea King; Myristicaceae; Acylphenols; Dimeric acylphenols; Malabaricone E; Acetylcholinesterase enzyme; Butyrylcholinesterase enzyme
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science > Dept of Chemistry
Depositing User: Ms. Juhaida Abd Rahim
Date Deposited: 12 Oct 2017 02:53
Last Modified: 01 Mar 2019 09:14
URI: http://eprints.um.edu.my/id/eprint/17980

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