Inhibitory effects of sulfenimides on human and bovine carbonic anhydrase enzymes

Yakan H., Bilir G., Çakmak Ş., Taş Ö., Türköz Karakullukçu N., Soydan E., ...Daha Fazla

Journal of Enzyme Inhibition and Medicinal Chemistry, cilt.38, sa.1, 2023 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 38 Sayı: 1
  • Basım Tarihi: 2023
  • Doi Numarası: 10.1080/14756366.2023.2194573
  • Dergi Adı: Journal of Enzyme Inhibition and Medicinal Chemistry
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, BIOSIS, Chemical Abstracts Core, EMBASE, Food Science & Technology Abstracts, MEDLINE, Directory of Open Access Journals
  • Anahtar Kelimeler: Carbonic anhydrase, inhibitor, sulfenimide, phthalimide, thiophenol, MICROWAVE-ASSISTED SYNTHESIS, BIOLOGICAL EVALUATION, ISOFORMS I, DERIVATIVES, DESIGN, SULFONAMIDES, CHEMISTRY
  • Eskişehir Osmangazi Üniversitesi Adresli: Evet

Özet

A series of sulfenimide derivatives (1a-i) were investigated as inhibitors of human (hCA-I, hCA-II) and bovine (bCA) carbonic anhydrase enzymes. The compounds were synthesised by the reaction of substituted thiophenols with phthalimide by means of an effective, simple and eco-friendly method and the structures were confirmed by IR, 1H NMR, 13C NMR, MS and elemental analysis. All derivatives except for the methyl derivative (1b) exhibited effective inhibitory action at low micromolar concentrations on human isoforms, but only four derivatives (1e, 1f, 1h, 1i) inhibited the bovine enzyme. The bromo derivative (1f) was found to be strongest inhibitor of all three enzymes with KI values of 0.023, 0.044 and 20.57 µM for hCA-I, hCA-II and bCA, respectively. Results of our study will make valuable contributions to carbonic anhydrase inhibition studies for further investigations since inhibitors of this enzyme are important molecules for medicinal chemistry.