Novel carvacrol based new oxypropanolamine derivatives: Design, synthesis, characterization, biological evaluation, and molecular docking studies

Bytyqi-Damoni A., Kestane A., Taslimi P., TÜZÜN B., Zengin M., Bilgicli H. G., ...Daha Fazla

Journal of Molecular Structure, cilt.1202, 2020 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 1202
  • Basım Tarihi: 2020
  • Doi Numarası: 10.1016/j.molstruc.2019.127297
  • Dergi Adı: Journal of Molecular Structure
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Chimica, Compendex, INSPEC
  • Anahtar Kelimeler: Oxypropanolamine, Acetylcholinesterase, Carbonic anhydrase, Enzyme inhibition, Molecular docking, ANHYDRASE INHIBITORY PROPERTIES, POTENT CARBONIC-ANHYDRASE, IN-VITRO INHIBITION, CRYSTAL-STRUCTURE, ALPHA-GLUCOSIDASE, NATURAL-PRODUCTS, AROMATIC PLANTS, ACETYLCHOLINESTERASE, ENZYME, SALTS
  • Atatürk Üniversitesi Adresli: Evet

Özet

Carvacrol, as a natural product used for many years in the treatment of various diseases, therefore it was chosen as the starting compound for this study. Novel carvacrol based new oxypropanolamine derivatives were synthesized and characterized by spectroscopic methods. All new compounds were tested as metabolic enzyme inhibitory agents. Their clinical usage of carvacrol has been established as diuretics, antiepileptics, and anti-glaucoma factors, in the management of gastric, duodenal ulcers, mountain sickness, osteoporosis, idiopathic intracranial hypertension, or neurological disorders. The in vitro anti-hyperglycemic screening results showed that the compound 3d exhibits the maximum inhibitory effect against alpha-glycosidase enzyme (IC50: 904.10 nM). In addition, the compounds 3d (IC50: 29.74 nM and 23.64 nM) and 3e (IC50: 31.28 nM and 26.11 nM) were found to have a significant response to inhibit carbonic anhydrase I, and II isoenzymes (hCA I and II), respectively. The novel carvacrol based oxypropanolamine compounds were effective inhibitors of the hCA I and II isozymes, and acetylcholinesterase with Ki values in the range of 27.18-44.84 nM for hCA I, 25.62-38.71 nM for hCA II, and 99.83-146.25 nM for AChE, respectively. (C) 2019 Elsevier B.V. All rights reserved.y