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Inhibitory effects of sulfenimides on human and bovine carbonic anhydrase enzymes.
Yakan, Hasan; Bilir, Gürkan; Çakmak, Sükriye; Tas, Ömer; Türköz Karakullukçu, Nalan; Soydan, Ercan; Kütük, Halil; Güçlü, Coskun; Sentürk, Murat; Arslan, Tayfun; Öztürk, Seyhan; Aksakal, Ercüment; Ekinci, Deniz.
Afiliación
  • Yakan H; Faculty of Education, Department of Science and Mathematics Education, Ondokuz Mayis University, Samsun, Türkiye.
  • Bilir G; Faculty of Agriculture, Department of Agricultural Biotechnology, Ondokuz Mayis University, Samsun, Türkiye.
  • Çakmak S; Vocational School, Environmental Health Programme, Sinop University, Sinop, Türkiye.
  • Tas Ö; Faculty of Agriculture, Department of Agricultural Biotechnology, Ondokuz Mayis University, Samsun, Türkiye.
  • Türköz Karakullukçu N; Karadeniz Advanced Technology Research and Application Centre, Ondokuz Mayis University, Samsun, Türkiye.
  • Soydan E; Faculty of Agriculture, Department of Agricultural Biotechnology, Ondokuz Mayis University, Samsun, Türkiye.
  • Kütük H; Faculty of Arts and Sciences, Department of Chemistry, Ondokuz Mayis University, Samsun, Türkiye.
  • Güçlü C; Faculty of Agriculture, Department of Agricultural Biotechnology, Eskisehir Osmangazi University, Eskisehir, Türkiye.
  • Sentürk M; Department of Biochemistry, Faculty of Paharnacy, Agri Ibrahim Cecen University, Agri, Türkiye.
  • Arslan T; Department of Chemistry, Faculty of Arts and Sciences, Giresun University, Giresun, Türkiye.
  • Öztürk S; Faculty of Arts and Sciences, Department of Chemistry, Ondokuz Mayis University, Samsun, Türkiye.
  • Aksakal E; Department of Agricultural Biotechnology, Division of Animal Biotechnology, Agriculture Faculty, Akdeniz University, Antalya, Türkiye.
  • Ekinci D; Faculty of Agriculture, Department of Agricultural Biotechnology, Ondokuz Mayis University, Samsun, Türkiye.
J Enzyme Inhib Med Chem ; 38(1): 2194573, 2023 Dec.
Article en En | MEDLINE | ID: mdl-36971264
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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Anhidrasas Carbónicas Límite: Animals / Humans Idioma: En Revista: J Enzyme Inhib Med Chem Asunto de la revista: BIOQUIMICA / QUIMICA Año: 2023 Tipo del documento: Article Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Anhidrasas Carbónicas Límite: Animals / Humans Idioma: En Revista: J Enzyme Inhib Med Chem Asunto de la revista: BIOQUIMICA / QUIMICA Año: 2023 Tipo del documento: Article Pais de publicación: Reino Unido