The synthesis of (Z)-4-oxo-4-(arylamino)but-2-enoic acids derivatives and determination of their inhibition properties against human carbonic anhydrase I and II isoenzymes |
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| Authors: | Koray Oktay Leyla Polat Köse K?v?lc?m ?endil Claudiu T Supuran |
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| Institution: | 1. Faculty of Science, Department of Chemistry, Ataturk University, Erzurum, Turkey,;2. Faculty of Science and Arts, Department of Chemistry, Kafkas University, Kars, Turkey,;3. Dipartimento di Chimica Ugo Schiff, Università degli Studi di Firenze, Sesto Fiorentino (Firenze), Italy, and;4. Neurofarba Department, Section of Pharmaceutical and Nutriceutical Sciences, Università degli Studi di Firenze, Sesto Fiorentino (Florence), Italy |
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| Abstract: | The synthesis of (Z)-4-oxo-4-(arylamino)but-2-enoic acid (4) derivatives containing structural characteristics that can be used for the synthesis of several active molecules, is presented. Some of the butenoic acid derivatives (4a, 4c, 4e, 4i, 4j, 4k) are synthesized following literature procedures and at the end of the reaction. In addition, structures of all synthesized derivatives (4a–4m) were determined by 1H-NMR, 13C-NMR and IR spectroscopy. Carbonic anhydrase is a metalloenzyme involved in many crucial physiologic processes as it catalyzes a simple but fundamental reaction, the reversible hydration of carbon dioxide to bicarbonate and protons. Significant results were obtained by evaluating the enzyme inhibitory activities of these derivatives against human carbonic anhydrase hCA I and II isoenzymes (hCA I and II). Butenoic acid derivatives (4a–4m) strongly inhibited hCA I and II 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. |
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| Keywords: | Butenoic acid carbonic anhydrase enzyme inhibition enzyme purification isoenzymes |
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