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Molecules 2017, 22(6), 1005;

Cholinesterase Inhibitory Activities of Adamantyl-Based Derivatives and Their Molecular Docking Studies

School of Chemical Sciences, Universiti Sains Malaysia, Penang 11800 USM, Malaysia
School of Biosciences, Taylor’s University, Lakeside Campus, 47500 Subang Jaya, Selangor, Malaysia
X-ray Crystallography Unit, School of Physics, Universiti Sains Malaysia, Penang 11800 USM, Malaysia
Department of Engineering Chemistry, Vidya Vikas Institute of Engineering & Technology, Visvesvaraya Technological University, Alanahalli, Mysuru 570028, Karnataka, India
Author to whom correspondence should be addressed.
Academic Editors: Anthony H. Futerman, Yacov Ashani, Gabriel (Gabi) Amitai and Lev Weiner
Received: 23 May 2017 / Revised: 10 June 2017 / Accepted: 14 June 2017 / Published: 17 June 2017
Full-Text   |   PDF [2888 KB, uploaded 17 June 2017]   |  


Adamantyl-based compounds are clinically important for the treatments of type 2 diabetes and for their antiviral abilities, while many more are under development for other pharmaceutical uses. This study focused on the acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibitory activities of adamantyl-based ester derivatives with various substituents on the phenyl ring using Ellman’s colorimetric method. Compound 2e with a 2,4-dichloro electron-withdrawing substituent on the phenyl ring exhibited the strongest inhibition effect against AChE, with an IC50 value of 77.15 µM. Overall, the adamantyl-based ester with the mono-substituent at position 3 of the phenyl ring exhibited good AChE inhibition effects with an ascending order for the substituents: Cl < NO2 < CH3 < OCH3. Furthermore, compounds with electron-withdrawing groups (Cl and NO2) substituted at position 3 on their phenyl rings demonstrated stronger AChE inhibition effects, in comparison to their respective positional isomers. On the other hand, compound 2j with a 3-methoxyphenyl ring showed the highest inhibition effect against BChE, with an IC50 value of 223.30 µM. Molecular docking analyses were conducted for potential AChE and BChE inhibitors, and the results demonstrated that the peripheral anionic sites of target proteins were predominant binding sites for these compounds through hydrogen bonds and halogen interactions instead of hydrophobic interactions in the catalytic active site. View Full-Text
Keywords: adamantane; acetylcholinesterase; butyrylcholinesterase; molecular docking adamantane; acetylcholinesterase; butyrylcholinesterase; molecular docking

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Kwong, H.C.; Mah, S.H.; Chia, T.S.; Quah, C.K.; Lim, G.K.; Kumar, C.S.C. Cholinesterase Inhibitory Activities of Adamantyl-Based Derivatives and Their Molecular Docking Studies. Molecules 2017, 22, 1005.

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