Synthesis and biological evaluation of 2,5-disubstituted furan derivatives containing 1,3-thiazole moiety as potential α-glucosidase inhibitors

Bioorg Med Chem Lett. 2023 Mar 1:83:129173. doi: 10.1016/j.bmcl.2023.129173. Epub 2023 Feb 9.

Abstract

α-Glucosidase, which is involved in the hydrolysis of carbohydrates to glucose and directly mediates blood glucose elevation, is a crucial therapeutic target for type 2 diabetes. In this work, 2,5-disubstituted furan derivatives containing 1,3-thiazole-2-amino or 1,3-thiazole-2-thiol moiety (III-01 ∼ III-30) were synthesized and screened for their inhibitory activity against α-glucosidase. α-Glucosidase inhibition assay demonstrated that all compounds had IC50 in the range of 0.645-94.033 μM and more potent than standard inhibitor acarbose (IC50 = 452.243 ± 54.142 µM). The most promising inhibitors of the two series were compound III-10 (IC50 = 4.120 ± 0.764 μM) and III-24 (IC50 = 0.645 ± 0.052 μM), respectively. Kinetic study and molecular docking simulation revealed that compound III-10 (Ki = 2.04 ± 0.72 μM) is a competitive inhibitor and III-24 (Ki = 0.44 ± 0.53 μM) is a noncompetitive inhibitor against α-glucosidase. Significantly, these two compounds showed nontoxicity towards HEK293, RAW264.7 and HepG2 cells, suggesting that compounds may be considered as a class of potential candidates for further developing novel antidiabetic drugs.

Keywords: 1,3-Thiazole; 2,5-Disubstituted furan; Molecular docking; Structure-activity relationship; α-Glucosidase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Diabetes Mellitus, Type 2*
  • Furans / chemistry
  • Glycoside Hydrolase Inhibitors* / pharmacology
  • HEK293 Cells
  • Humans
  • Kinetics
  • Molecular Docking Simulation
  • Molecular Structure
  • Structure-Activity Relationship
  • Thiazoles / pharmacology
  • alpha-Glucosidases / metabolism

Substances

  • alpha-Glucosidases
  • Glycoside Hydrolase Inhibitors
  • Thiazoles
  • Furans