Synthesis, Molecular Docking Analysis, and Carbonic Anhydrase Inhibitory Evaluations of Benzenesulfonamide Derivatives Containing Thiazolidinone

Molecules. 2019 Jun 30;24(13):2418. doi: 10.3390/molecules24132418.

Abstract

To find novel human carbonic anhydrase (hCA) inhibitors, we synthesized thirteen compounds by combining thiazolidinone with benzenesulfonamide. The result of the X-ray single-crystal diffraction experiment confirmed the configuration of this class of compounds. The enzyme inhibition assays against hCA II and IX showed desirable potency profiles, as effective as the positive controls. The docking studies revealed that compounds (2) and (7) efficiently bound in the active site cavity of hCA IX by forming sufficient interactions with active site residues. The fragment of thiazolidinone played an important role in the binding of the molecules to the active site.

Keywords: benzenesulfonamide; docking study; human carbonic anhydrase IX; thiazolidinone.

MeSH terms

  • Antigens, Neoplasm* / chemistry
  • Benzenesulfonamides
  • Carbonic Anhydrase II* / antagonists & inhibitors
  • Carbonic Anhydrase II* / chemistry
  • Carbonic Anhydrase IX* / antagonists & inhibitors
  • Carbonic Anhydrase IX* / chemistry
  • Carbonic Anhydrase Inhibitors* / chemical synthesis
  • Carbonic Anhydrase Inhibitors* / chemistry
  • Catalytic Domain
  • Humans
  • Molecular Docking Simulation*
  • Sulfonamides* / chemical synthesis
  • Sulfonamides* / chemistry

Substances

  • Antigens, Neoplasm
  • Carbonic Anhydrase Inhibitors
  • Sulfonamides
  • Carbonic Anhydrase II
  • CA2 protein, human
  • CA9 protein, human
  • Carbonic Anhydrase IX