2. Academic Validation
  3. Inhibitory effects of sulfenimides on human and bovine carbonic anhydrase enzymes

Inhibitory effects of sulfenimides on human and bovine carbonic anhydrase enzymes

  • J Enzyme Inhib Med Chem. 2023 Dec;38(1):2194573. doi: 10.1080/14756366.2023.2194573.
Hasan Yakan 1,  Gürkan Bilir 2,  Şükriye Çakmak 3,  Ömer Taş 2,  Nalan Türköz Karakullukçu 4,  Ercan Soydan 2,  Halil Kütük 5,  Coşkun Güçlü 6,  Murat Şentürk 7,  Tayfun Arslan 8,  Seyhan Öztürk 5,  Ercüment Aksakal 9,  Deniz Ekinci 2
Affiliations

Affiliations

  • 1 Faculty of Education, Department of Science and Mathematics Education, Ondokuz Mayis University, Samsun, Türkiye.
  • 2 Faculty of Agriculture, Department of Agricultural Biotechnology, Ondokuz Mayıs University, Samsun, Türkiye.
  • 3 Vocational School, Environmental Health Programme, Sinop University, Sinop, Türkiye.
  • 4 Karadeniz Advanced Technology Research and Application Centre, Ondokuz Mayis University, Samsun, Türkiye.
  • 5 Faculty of Arts and Sciences, Department of Chemistry, Ondokuz Mayis University, Samsun, Türkiye.
  • 6 Faculty of Agriculture, Department of Agricultural Biotechnology, Eskisehir Osmangazi University, Eskisehir, Türkiye.
  • 7 Department of Biochemistry, Faculty of Paharnacy, Agri Ibrahim Cecen University, Agri, Türkiye.
  • 8 Department of Chemistry, Faculty of Arts and Sciences, Giresun University, Giresun, Türkiye.
  • 9 Department of Agricultural Biotechnology, Division of Animal Biotechnology, Agriculture Faculty, Akdeniz University, Antalya, Türkiye.
PMID: 36971264 DOI: 10.1080/14756366.2023.2194573
Abstract

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.

Keywords

Carbonic anhydrase; inhibitor; phthalimide; sulfenimide; thiophenol.

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