Cholinesterases, alpha-glycosidase, and carbonic anhydrase inhibition properties of 1H-pyrazolo[1,2-b]phthalazine-5,10-dione derivatives: Synthetic analogues for the treatment of Alzheimer's disease and diabetes mellitus

Taslimi P., TURHAN K., Turkan F., Karaman H. S., TURGUT Z., GÜLÇİN İ.

BIOORGANIC CHEMISTRY, vol.97, 2020 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 97
  • Publication Date: 2020
  • Doi Number: 10.1016/j.bioorg.2020.103647
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Chimica, EMBASE, MEDLINE, Veterinary Science Database
  • Keywords: 1H-pyrazolo[1, 2-b]phthalazine-5, 10-dione, Cholinesterase, Carbonic anhydrase, alpha-glycosidase, Molecular docking, GLUTATHIONE-S-TRANSFERASE, MOLECULAR DOCKING, ACETYLCHOLINESTERASE, BUTYRYLCHOLINESTERASE, LACTOPEROXIDASE, ENZYME, ACHE
  • Yıldız Technical University Affiliated: Yes


In this study, using the Cu(OTf)(2) catalyst, 1H-pyrazolo[1,2-b]phthalazine-5,10-dione derivative molecules were carried out in one step and with high yield (86-91%). The previously synthesized 1H-pyrazolo [1,2-b]phthalazine-5,10-dione derivatives, carbonic anhydrase I and II isozymes (hCA I and II), acetylcholinesterase (AChE), butyrylcholinesterase (BChE) and alpha-glycosidase (alpha-Gly) enzymes with K-i values in the range of 4.88-15.94 nM for hCA I, 7.04-20.83 nM for hCA II, 68.25-158.27 for AChE, 60.17-91.27 for BChE and 0.36-2.36 nM for alpha-Gly, respectively. In silico studies were performed on the molecules inhibiting hCA I, hCA II, AChE, BChE and alpha-Gly receptors. When we evaluated the data obtained in this work, we determined the inhibition type of the 1H-pyrazolo[1,2-b]phthalazine-5,10-dione derivatives at the receptors. Reference inhibitors were used for all enzymes.