Synthesis, characterization and carbonic anhydrase inhibitory activity of novel benzothiazole derivatives

KÜÇÜKBAY F., BUGDAY N., Kucukbay H., TANC M., SUPURAN C. T.

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, vol.31, no.6, pp.1221-1225, 2016 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 31 Issue: 6
  • Publication Date: 2016
  • Doi Number: 10.3109/14756366.2015.1114931
  • Journal Name: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.1221-1225
  • Keywords: Amino acid-benzothiazole conjugates, benzothiazole, carbonic anhydrase, ANTIMICROBIAL ACTIVITY, DISCOVERY, BIOASSAY, AGENTS, DRUGS
  • Inonu University Affiliated: Yes

Abstract

N-protected amino acids were reacted with substituted benzothiazoles to give the corresponding N-protected amino acid-benzothiazole conjugates (60-89%). Their structures were confirmed by proton nuclear magnetic resonance (H-1 NMR), carbon-13 nuclear magnetic resonance (C-13 NMR), IR and elemental analysis. Their carbonic anhydrase (CA, EC 4.2.1.1) inhibitory activities were determined against two cytosolic human isoforms (hCA I and hCA II), one membrane-associated (hCA IV) and one transmembrane (hCA XII) enzyme by a stopped-flow CO2 hydrase assay method. The new compounds showed rather weak, micromolar inhibitory activity against most of these enzymes.