石杉碱甲
乙酰胆碱酯酶
对接(动物)
乙酰胆碱酯酶抑制剂
化学
阿切
药理学
酶
丁酰胆碱酯酶
立体化学
生物化学
医学
护理部
作者
Anwar Alam,Sibhghatulla Shaikh,Syed Sayeed Ahmad,Mohammad A. Ansari,Shahnawaz Shakil,Syed Mohd Danish Rizvi,Shazi Shakil,Mohammad Imran,Mohammad Haneef,Adel M. Abuzenadah,Mohammad Amjad Kamal
出处
期刊:Cns & Neurological Disorders-drug Targets
[Bentham Science]
日期:2014-05-31
卷期号:13 (3): 487-490
被引量:18
标识
DOI:10.2174/18715273113126660163
摘要
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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