Intermolecular amination of allylic and benzylic alcohols leads to effective inhibitions of acetylcholinesterase enzyme and carbonic anhydrase I and II isoenzymes

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Atmaca U., Yıldırım A., Taslimi P., Çelik S. T., Gulcin İ., Supuran C. T., ...Daha Fazla

JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY, cilt.32, sa.8, 2018 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 32 Sayı: 8
  • Basım Tarihi: 2018
  • Doi Numarası: 10.1002/jbt.22173
  • Dergi Adı: JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Anahtar Kelimeler: acetylcholinesterase, amination, carbonic anhydrase, sulfamate, sulfonamide, GLUTATHIONE-S-TRANSFERASE, ERYTHROCYTE ISOZYMES I, ANTICHOLINERGIC PROPERTIES, SULFONAMIDE DERIVATIVES, CRYSTAL-STRUCTURE, MANNICH-BASES, HCA I, ANTIOXIDANT, BUTYRYLCHOLINESTERASE, POTENT
  • Atatürk Üniversitesi Adresli: Evet

Özet

In this study, we aimed to determine the inhibition effects of novel synthesized sulfamates (2a-g), sulfonamides (3b-f). carbonyl sulfonamides (3h and i). and carbonyl sulfamates (4h and 4i), which were tested against two human cytosolic carbonic anhydrase I and II isozymes (hCA I and II) and acetylcholinesterase (AChE) enzyme. For inhibition properties of allylic sulfamates, the half maximal inhibitory concentration (IC50) and inhibition constant (K-i) were calculated for each novel compounds. The allylic sulfamates showed that K-i values are in the range of 187.33-510.31 pM for hCA I. 104.22 -290.09 pM against hCA II, and 12.73-103.63 pM against AChE. The results demonstrated that all newly synthesized compounds had shown effective inhibition against hCA I and II isoenzymes and AChE enzyme.