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, DOI https://doi.org/10.1016/j.bmcl.2016.05.046.
Full text not available from this repository.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 |
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Funders: | University of Malaya Research Grant RP001-2012A/B , Centre National de la Recherche Scientifique (CNRS) grant (57-02-03-1007) |
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 > Department 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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