Synthesis of 2‐amino‐3‐cyanopyridine derivatives and investigation of their carbonic anhydrase inhibition effects |
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Authors: | Aliye Altundas Berna Gül Murat Çankaya Ali Atasever İlhami Gülçin |
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Affiliation: | 1. Department of Chemistry, Faculty of Science and Arts, Gazi University, Ankara, Turkey;2. Department of Biology, Faculty of Science and Arts, Erzincan University, Erzincan, Turkey;3. Department of Food Science, Ispir H. Polat Vocational School, Atatürk University, Erzurum, Turkey;4. Department of Chemistry, Faculty of Science, Atatürk University, Erzurum, Turkey |
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Abstract: | The conversion of carbon dioxide (CO2) and bicarbonate (HCO3−) to each other is very important for living metabolism. Carbonic anhydrase (CA, E.C.4.2.1.1), a metalloenzyme familly, catalyzes the interconversion of these ions (CO2 and HCO3−) and are very common in living organisms. In this study, a series of novel 2‐amino‐3‐cyanopyridines supported with some functional groups was synthesized and tested as potential inhibition effects against both cytosolic human CA I and II isoenzymes (hCA I and II) using by Sepharose‐4B‐l ‐tyrosine‐sulfanilamide affinity chromatography. The structural elucidations of novel 2‐amino‐3‐cyanopyridines were achieved by NMR, IR, and elemental analyses. K i values of the novel synthesized compounds were found in range of 2.84–112.44 μM against hCA I and 2.56–31.17 μM against hCA II isoenzyme. While compound 7d showed the best inhibition activity against hCA I (K i: 2.84 μM), the compound 7b demonstrated the best inhibition profile against hCA II isoenzyme (K i: 2.56 μM). |
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Keywords: | 2‐amino‐3‐cyanopyridine carbonic anhydrase enzyme purification enzyme inhibition |
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