Natural cholinesterase inhibitors from Myristica cinnamomea King
Document Type
Article
Publication Date
1-1-2016
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.
Keywords
Myristica cinnamomea King, Myristicaceae, Acylphenols, Dimeric acylphenols, Malabaricone E, Acetylcholinesterase enzyme, Butyrylcholinesterase enzyme
Publication Title
Bioorganic & Medicinal Chemistry Letters
Divisions
CHEMISTRY
Funders
University of Malaya Research Grant RP001-2012A/B ,Centre National de la Recherche Scientifique (CNRS) grant (57-02-03-1007)
Volume
26
Issue
15
Publisher
Elsevier