Synthesis of 2-amino-3-cyanopyridine derivatives and investigation of their carbonic anhydrase inhibition effects
JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY, cilt.31, sa.12, 2017 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 31 Sayı: 12
- Basım Tarihi: 2017
- Doi Numarası: 10.1002/jbt.21998
- Dergi Adı: JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Anahtar Kelimeler: 2-amino-3-cyanopyridine, carbonic anhydrase, enzyme purification, enzyme inhibition, GLUTATHIONE-S-TRANSFERASE, ISOENZYMES HCA I, ISOZYMES I, ACETYLCHOLINESTERASE, BUTYRYLCHOLINESTERASE, LACTOPEROXIDASE, BROMOPHENOLS, PROFILES, SERIES, CYTOTOXICITY
- Gazi Üniversitesi Adresli: Evet
Özet
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 2.84-112.44M against hCA I and 2.56-31.17M against hCA II isoenzyme. While compound 7d showed the best inhibition activity against hCA I (K-i: 2.84M), the compound 7b demonstrated the best inhibition profile against hCA II isoenzyme (K-i: 2.56M).