Synthesis and discovery of potent carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase, and α-glycosidase enzymes inhibitors: The novel N,N′-bis-cyanomethylamine and alkoxymethylamine derivatives


Taslimi P., ÇAĞLAYAN C., Farzaliyev V., Nabiyev O., Sujayev A., Turkan F., ...Daha Fazla

Journal of Biochemical and Molecular Toxicology, cilt.32, sa.4, 2018 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 32 Sayı: 4
  • Basım Tarihi: 2018
  • Doi Numarası: 10.1002/jbt.22042
  • Dergi Adı: Journal of Biochemical and Molecular Toxicology
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Anahtar Kelimeler: acetylcholinesterase, butyrylcholinesterase, carbonic anhydrase, enzyme inhibition, N,N′-bis-cyanomethylamine
  • Bilecik Şeyh Edebali Üniversitesi Adresli: Hayır

Özet

During this investigation, N,N′-bis-azidomethylamines, N,N′-bis-cyanomethylamine, new alkoxymethylamine and chiral derivatives, which are considered to be a new generation of multifunctional compounds, were synthesized, functional properties were investigated, and anticholinergic and antidiabetic properties of those compounds were studied through the laboratory tests, and it was approved that they contain physiologically active compounds rather than analogues. Novel N-bis-cyanomethylamine and alkoxymethylamine derivatives were effective inhibitors of the α-glycosidase, cytosolic carbonic anhydrase I and II isoforms, butyrylcholinesterase (BChE), and acetylcholinesterase (AChE) with Ki values in the range of 0.15–13.31 nM for α-glycosidase, 2.77–15.30 nM for human carbonic anhydrase isoenzymes I (hCA I), 3.12–21.90 nM for human carbonic anhydrase isoenzymes II (hCA II), 23.33–73.23 nM for AChE, and 3.84–48.41 nM for BChE, respectively. Indeed, the inhibition of these metabolic enzymes has been considered as a promising factor for pharmacologic intervention in a diversity of disturbances.