Molecular Interaction of Human Brain Acetylcholinesterase with a Natural Inhibitor Huperzine-B: An Enzoinformatics Approach

ISSN: 1996-3181 (Online)
ISSN: 1871-5273 (Print)


Volume 13, 10 Issues, 2014


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CNS & Neurological Disorders - Drug Targets

Formerly: Current Drug Targets - CNS & Neurological Disorders

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  • 78th of 252 in Neurosciences

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Editor-in-Chief:
Stephen D. Skaper
Department of Pharmaceutical and Pharmacological Sciences
University of Padova
Padova
Italy


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Molecular Interaction of Human Brain Acetylcholinesterase with a Natural Inhibitor Huperzine-B: An Enzoinformatics Approach

Author(s): Aftab Alam, Sibhghatulla Shaikh, Syed S. Ahmad, Mohammad A. Ansari, Shahnawaz Shakil, Syed M.D. Rizvi, Shazi Shakil, Mohammad Imran, Mohammad Haneef, Adel M. Abuzenadah and Mohammad A. Kamal

Affiliation: Department of Bio-Engineering, Integral University, Lucknow-226026, India.

Abstract

The present study emphasizes the molecular interactions between human brain acetylcholinesterase (AChE) and the natural ligand Huperzine-B and its comparison to ‘AChE-Tolserine interactions’. Docking between Huperzine-B and AChE was performed using ‘Autodock4.2’. Hydrophobic interactions and hydrogen bonds both play an equally important role in the correct positioning of Huperzine-B within the ‘catalytic site’ of AChE to permit docking. However, docking of Tolserine to AChE is largely dominated by hydrophobic interactions. Such information may aid in the design of versatile AChE-inhibitors, and is expected to aid in safe clinical use of Huperzine-B. Scope still remains in the determination of the three-dimensional structure of AChE-Huperzine-B complex by X-ray crystallography to validate the described data. Furthermore, this study confirms that Huperzine-B is a more efficient inhibitor of human brain AChE compared to tolserine with reference to Ki and ΔG values.

Keywords: Acetylcholinesterase, autodock4.2, hydrophobic interactions, catalytic site.

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Article Details

Volume: 13
Issue Number: 3
First Page: 487
Last Page: 490
Page Count: 4
DOI: 10.2174/18715273113126660163
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