Tehran University of Medical Sciences

Science Communicator Platform

Stay connected! Follow us on X network (Twitter):
Share this content! On (X network) By
A New Route to the Synthesis of 2-Hydrazolyl-4-Thiazolidinone Hybrids, Evaluation of Α-Glucosidase Inhibitory Activity and Molecular Modeling Insights Publisher



Sepehri S1, 2 ; Farhadi G3 ; Maghbul M4 ; Nasiri F4 ; Faramarzi MA5 ; Mahnam K6 ; Mojtabavi S5 ; Mahdavi M7 ; Moharrami Oranj Z4
Authors
Show Affiliations
Authors Affiliations
  1. 1. Pharmaceutical Sciences Research Center, Ardabil University of Medical Sciences, Ardabil, Iran
  2. 2. Department of Medicinal Chemistry, School of Pharmacy, Ardabil University of Medical Sciences, Ardabil, Iran
  3. 3. Students Research Committee, School of Pharmacy, Ardabil University of Medical Sciences, Ardabil, Iran
  4. 4. Department of Applied Chemistry, University of Mohaghegh Ardabili, Ardabil, Iran
  5. 5. Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran
  6. 6. Department of Biology, Faculty of Sciences, Shahrekord University, Shahrekord, Iran
  7. 7. Endocrinology and Metabolism Research Center, Endocrinology and Metabolism Clinical Sciences Institute, Tehran University of Medical Sciences, Tehran, Iran

Source: Heliyon Published:2024


Abstract

One of the multifactorial worldwide health syndromes is diabetes mellitus which is increasing at a disturbing rate. The inhibition of α-glucosidase, an enzyme that catalyzes starch hydrolysis in the intestine, is one helpful therapeutic approach for controlling hyperglycemia related to type-2 diabetes. To discover α-glucosidase inhibitors, some 2-hydrazolyl-4-thiazolidinone hybrids (3a-e) were synthesized from new one-pot reaction procedures. Next, their chemical structures were confirmed by 1H NMR, 13C NMR, and FT-IR spectra, and elemental analysis technique. Then, the α-glucosidase inhibitory activity of the titled compounds was evaluated. Among them, derivatives 3b and 3c revealed the highest activity against α-glucosidase compared to acarbose as a drug. Enzyme kinetic studies of the most active derivative (3b) indicated a competitive inhibition. Finally, molecular modeling studies were accomplished to describe vital interactions of the most potent compounds (3b and 3c) with the α-glucosidase enzyme. © 2024 The Authors