Synthesis and molecular docking studies of potent α-glucosidase inhibitors based on biscoumarin skeleton

Khan KM 1 , Rahim F 2 , Wadood A 3 , Kosar N 2 , Taha M 4 , Lalani S 5 Show all authors , Khan A 2 , Fakhri MI 5 , Junaid M 3 , Rehman W 2 , Khan M 6 , Perveen S 7 , Sajid M 8 , Choudhary MI 5

Affiliations 

  • 1 H.E.J. Research Institute of Chemistry, International Center for Chemical and Biological Sciences, University of Karachi, Karachi 75270, Pakistan. Electronic address: khalid.khan@iccs.edu
  • 2 Department of Chemistry, Hazara University, Mansehra, Pakistan
  • 3 Computational Medicinal Chemistry Laboratory, Department of Biochemistry, Abdul Wali Khan University, Mardan, Mardan 23200, Pakistan
  • 4 Atta-ur-Rahman Institute for Natural Product Discovery, Universiti Teknologi MARA (UiTM), Puncak Alam Campus, 42300 Bandar Puncak Alam, Selangor, Malaysia; Faculty of Applied Science, Universiti Tecknologi MARA, 40450 Shah Alam, Selangor D.E., Malaysia
  • 5 H.E.J. Research Institute of Chemistry, International Center for Chemical and Biological Sciences, University of Karachi, Karachi 75270, Pakistan
  • 6 Department of Chemistry, Abdul Wali Khan University, Mardan, Mardan 23200, Pakistan
  • 7 PCSIR Laboratories Complex, Karachi, Shahrah-e-Dr. Salimuzzaman Siddiqui, Karachi 75280, Pakistan
  • 8 Department of Biochemistry, Hazara University, Mansehra, Pakistan
Eur J Med Chem, 2014 Jun 23;81:245-52.
PMID: 24844449 DOI: 10.1016/j.ejmech.2014.05.010

Abstract

In our effort directed toward the discovery of new anti-diabetic agent for the treatment of diabetes, a library of biscoumarin derivative 1-18 was synthesized and evaluated for α-glucosidase inhibitory potential. All eighteen (18) compounds displayed assorted α-glucosidase activity with IC50 values 16.5-385.9 μM, if compared with the standard acarbose (IC50 = 906 ± 6.387 μM). In addition, molecular docking studies were carried out to explore the binding interactions of biscoumarin derivatives with the enzyme. This study has identified a new class of potent α-glucosidase inhibitors.

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

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