2-Aryl benzimidazoles: Synthesis, In vitro α-amylase inhibitory activity, and molecular docking study

Adegboye AA 1 , Khan KM 2 , Salar U 3 , Aboaba SA 1 , Kanwal 3 , Chigurupati S 4 Show all authors , Fatima I 3 , Taha M 5 , Wadood A 6 , Mohammad JI 7 , Khan H 6 , Perveen S 8

Affiliations 

  • 1 Department of Chemistry, University of Ibadan, Ibadan, Nigeria
  • 2 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. Electronic address: khalid.khan@iccs.edu
  • 3 H. E. J. Research Institute of Chemistry, International Center for Chemical and Biological Sciences, University of Karachi, Karachi, 75270, Pakistan
  • 4 Department of Pharmaceutical Chemistry, Faculty of Pharmacy, AIMST University, Semeling, 08100 Bedong, Kedah, Malaysia
  • 5 Department of Clinical Pharmacy, Institute for Research and Medical Consultations (IRMC), Imam Abdulrahman Bin Faisal University, P.O. Box 1982, Dammam 31441, Saudi Arabia
  • 6 Department of Biochemistry, Computational Medicinal Chemistry Laboratory, UCSS, Abdul Wali Khan University, Mardan, Pakistan
  • 7 Department of Pharmacology, Faculty of Medicine, Cyberjaya University College of Medical Sciences, CUCMS, Cyberjaya, 63000, Malaysia
  • 8 PCSIR Laboratories Complex, Karachi, Shahrah-e-Dr. SalimuzzamanSiddiqui, Karachi, 75280, Pakistan
Eur J Med Chem, 2018 Apr 25;150:248-260.
PMID: 29533872 DOI: 10.1016/j.ejmech.2018.03.011

Abstract

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 IC50 values of 1.48 ± 0.38-2.99 ± 0.14 μM, when compared to the standard acarbose (IC50 = 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.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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