Chem. J. Chinese Universities ›› 2009, Vol. 30 ›› Issue (11): 2268.

• Articles • Previous Articles     Next Articles

Docking Studies on the Interaction of Imidazolines and Potassium Ion Channel-Kir6.2

ZHANG Rui1,3, LING Bao-Ping2, MENG Xiang-Hua2, WANG Zhi-Guo1,3, ZHANG Chang-Qiao2, LIU Yong-Jun1,2*, LIU Cheng-Bu2*   

  1. 1. Northwest Institute of Plateau Biology, Chinese Academy of Sciences, Xining 810001, China;
    2. School of Chemistry and Chemical Engineering, Shandong University, Jinan 250100, China;
    3. Graduate University of Chinese Academy of Science, Beijing 100049, China
  • Received:2008-11-17 Online:2009-11-10 Published:2009-11-10
  • Contact: LIU Yong-Jun, E-mail: yongjunliu1@sdu.edu.cn; LIU Cheng-Bu, E-mail: cbliu@sdu.edu.cn
  • Supported by:

    国家自然科学基金(批准号: 30873158)和国家“九七三”计划(批准号: 2008CB13617508)资助.

Abstract:

Kir6.2, a key component of the ATP-sensitive potassium channel(KATP), can directly interact with imidazolines, a kind of potential antidiabetic drug. This paper explored the interaction of Kir6.2 with imidazoline molecules by applying AutoDock software. The docking results reveal the binding sites of the seven imidazolines on Kir6.2. For Efaroxan, Clonidine, Cibenzoline and Bl11282, polar residues, H175, K67and W68, constitute the binding pocket; while Rx871024, Alinidine and Ly389382, lies in a hydrophobic pocket which is composed of nonpolar residues, F168, M169 and I296. Efaroxan, Clonidine, Cibenzoline and Bl11282 interact with Kir6.2 mainly by forming hydrogen bonds, but for Rx871024, Alinidine and Ly389382, the hydrophobic interaction is the most important mode of action. These binding sites and the interaction modes can interpret the inhibition of these imidazoline drugs to some extent, and this research may provide theoretical support in the pharmacological study of imidazolines regulating the secretion of insulin.

Key words: Imidazolines; KATP channel; Kir6.2; Docking; Binding site

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