CAJ | 학술논문

运用AutoDock4软件进行了分子对接研究, 得到了7种咪唑啉药物分子与Kir6.2的作用位点, 并发现了2个活性位点区域;依法可生(Efaroxan)、可乐定(Clonidine)、西苯唑啉(Cibenzoline)和Bl11282位于残基H175, K67和W68形成的活性口袋中, 主要作用方式为氢键相互作用;而Rx871024、烯丙尼定(Alinidine)和Ly389382位于残基F168, M169和I296形成的疏水口袋中, 在Kir6.2的通道孔中央, 没有氢键形成, 主要作用为疏水相互作用. 咪唑啉类药物与Kir6.2相互作用活性位点的理论预测将有助于该药物在胰腺β细胞中调控胰岛素分泌机制的研究.
운용AutoDock4연건진행료분자대접연구, 득도료7충미서람약물분자여Kir6.2적작용위점, 병발현료2개활성위점구역;의법가생(Efaroxan)、가악정(Clonidine)、서분서람(Cibenzoline)화Bl11282위우잔기H175, K67화W68형성적활성구대중, 주요작용방식위경건상호작용;이Rx871024、희병니정(Alinidine)화Ly389382위우잔기F168, M169화I296형성적소수구대중, 재Kir6.2적통도공중앙, 몰유경건형성, 주요작용위소수상호작용. 미서람류약물여Kir6.2상호작용활성위점적이론예측장유조우해약물재이선β세포중조공이도소분비궤제적연구.
Kir6.2, a key component of the ATP-sensitive potassium channel ( K_(ATP)),can directly interact with imidazolines, a kind of potential antidiabetic drug. This paper explored the interaction of Kir6.2 with im-idazoline molecules by applying AutoDock software. The docking results reveal the binding sites of the seven imidazolines on Kir6.2. For Efaroxan, Clonidine, Cibenzoline and 8111282, 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 B111282 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.