| Autor: |
Taslimi P; a Department of Chemistry , Faculty of Science, Atatürk University , Erzurum , Turkey ., Gülçin İ; a Department of Chemistry , Faculty of Science, Atatürk University , Erzurum , Turkey .; b Department of Zoology , College of Science, King Saud University , Riyadh , Saudi Arabia ., Öztaşkın N; a Department of Chemistry , Faculty of Science, Atatürk University , Erzurum , Turkey ., Çetinkaya Y; c Department of Food Technology , Oltu Vocational School, Atatürk University , Oltu , Erzurum , Turkey ., Göksu S; a Department of Chemistry , Faculty of Science, Atatürk University , Erzurum , Turkey ., Alwasel SH; b Department of Zoology , College of Science, King Saud University , Riyadh , Saudi Arabia ., Supuran CT; d Dipartimento di Chimica Ugo Schiff , Universita degli Studi di Firenze , Sesto Fiorentino , Firenze , Italy , and.; e Section of Pharmaceutical and Nutriceutical Sciences, Neurofarba Department, Universita Degli Studi di Firenze , Sesto Fiorentino , Florence , Italy. |
| Abstrakt: |
Carbonic anhydrases (CAs, EC 4.2.1.1), which are involved in a variety of physiological and pathological processes, are ubiquitous metalloenzymes mainly catalyzing the reversible hydration of carbon dioxide (CO2) to bicarbonate ([Formula: see text]) and proton (H(+)). In this study, a dozen of bromophenol derivatives (1-12) were evaluated as metalloenzyme CA (EC 4.2.1.1) inhibitors against the human carbonic anhydrase isoenzymes I and II (hCA I and II). Cytosolic hCA I and II isoenzymes were effectively inhibited by bromophenol derivatives (1-12) with Kis in the low nanomolar range of 1.85 ± 0.58 to 5.04 ± 1.46 nM against hCA I and in the range of 2.01 ± 0.52 to 2.94 ± 1.31 nM against hCA II, respectively. |
