2-芳基苯并咪唑：合成、体外α-淀粉酶抑制活性及分子对接研究
2-Aryl benzimidazoles: Synthesis, In vitro α-amylase inhibitory activity, and molecular docking study.
作者信息
Adegboye Akande Akinsola, Khan Khalid Mohammed, Salar Uzma, Aboaba Sherifat Adeyinka, Chigurupati Sridevi, Fatima Itrat, Taha Mohammad, Wadood Abdul, Mohammad Jahidul Isalm, Khan Huma, Perveen Shahnaz
机构信息
Department of Chemistry, University of Ibadan, Ibadan, Nigeria.
H. E. J. Research Institute of Chemistry, International Center for Chemical and Biological Sciences, University of Karachi, Karachi, 75270, Pakistan; Department of Clinical Pharmacy, Institute for Research and Medical Consultations (IRMC), Imam Abdulrahman Bin Faisal University, P.O. Box 1982, Dammam 31441, Saudi Arabia.
出版信息
Eur J Med Chem. 2018 Apr 25;150:248-260. doi: 10.1016/j.ejmech.2018.03.011. Epub 2018 Mar 6.
Despite of many diverse biological activities exhibited by benzimidazole scaffold, it is rarely explored for the α-amylase inhibitory activity. For that purpose, 2-aryl benzimidazole derivatives 1-45 were synthesized and screened for in vitro α-amylase inhibitory activity. Structures of all synthetic compounds were deduced by various spectroscopic techniques. All compounds revealed inhibition potential with IC values of 1.48 ± 0.38-2.99 ± 0.14 μM, when compared to the standard acarbose (IC = 1.46 ± 0.26 μM). Limited SAR suggested that the variation in the inhibitory activities of the compounds are the result of different substitutions on aryl ring. In order to rationalize the binding interactions of most active compounds with the active site of α-amylase enzyme, in silico study was conducted.
尽管苯并咪唑骨架具有多种不同的生物活性，但很少有人对其α-淀粉酶抑制活性进行研究。为此，合成了2-芳基苯并咪唑衍生物1-45，并对其体外α-淀粉酶抑制活性进行了筛选。通过各种光谱技术推导了所有合成化合物的结构。与标准阿卡波糖（IC = 1.46±0.26μM）相比，所有化合物的抑制潜力均显示IC值为1.48±0.38-2.99±0.14μM。有限的构效关系表明，化合物抑制活性的差异是芳环上不同取代的结果。为了阐明最具活性的化合物与α-淀粉酶活性位点的结合相互作用，进行了计算机模拟研究。
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