The green synthesis and molecular docking of novel N-substituted rhodanines as effective inhibitors for carbonic anhydrase and acetylcholinesterase enzymes

Bayindir S., Caglayan C., Karaman M., GÜLÇİN İ.

BIOORGANIC CHEMISTRY, cilt.90, 2019 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 90
  • Basım Tarihi: 2019
  • Doi Numarası: 10.1016/j.bioorg.2019.103096
  • Dergi Adı: BIOORGANIC CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Anahtar Kelimeler: Rhodanine, Aza-ylides, Acetylcholinesterase, Carbonic anhydrase, Enzyme inhibition, Molecular docking, TROUT ONCORHYNCHUS-MYKISS, ERYTHROCYTES IN-VITRO, ALZHEIMERS-DISEASE, CRYSTAL-STRUCTURE, BIOLOGICAL EVALUATION, ACHE INHIBITORS, DRUG DISCOVERY, 1ST SYNTHESIS, DERIVATIVES, BUTYRYLCHOLINESTERASE
  • Atatürk Üniversitesi Adresli: Evet

Özet

Recently, inhibition effects of enzymes such as acetylcholinesterase (AChE) and carbonic anhydrase (CA) has appeared as a promising approach for pharmacological intervention in a variety of disorders such as epilepsy, Alzheimer's disease and obesity. For this purpose, novel N-substituted rhodanine derivatives (RhAs) were synthesized by a green synthetic approach over one-pot reaction. Following synthesis the novel compounds, RhAs derivatives were tested against AChE and cytosolic carbonic anhydrase I, and II (hCAs I, and II) isoforms. As a result of this study, inhibition constant (Ki) were found in the range of 66.35 +/- 8.35 to 141.92 +/- 12.63 nM for AChE, 43.55 +/- 14.20 to 89.44 +/- 24.77 nM for hCA I, and 16.97 +/- 1.42 to 64.57 +/- 13.27 nM for hCA II, respectively. Binding energies were calculated with docking studies as -5.969, -5.981, and -9.121 kcal/mol for hCA I, hCA II, and AChE, respectively.