Cholinesterases, α-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

[Display omitted] •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%).•As a kinetic study, inhibition of the synthesized molecules on CA I, CA II, AAChE, BChE and α- Gly were performed.•They showed nanomolar inhibition levels on metabolic enzymes. 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 α-glycosidase (α-Gly) enzymes with Ki 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 α-Gly, respectively. In silico studies were performed on the molecules inhibiting hCA I, hCA II, AChE, BChE and α-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.