Taslimi, ParhamTurkan, FikretCetin, AdnanBurhan, HakanKaraman, MuhammetBildirici, IshakSen, Fatih2025-05-102025-05-1020190045-20681090-212010.1016/j.bioorg.2019.1032132-s2.0-85071275433https://doi.org/10.1016/j.bioorg.2019.103213https://hdl.handle.net/20.500.14720/11538Gulcin, Ilhami/0000-0001-5993-1668; Karaman, Muhammet/0000-0002-0155-3390; Sen, Fatih/0000-0001-9929-9556; Cetin, Adnan/0000-0003-4838-1503; Taslimi, Parham/0000-0002-3171-0633; Bildirici, Ishak/0000-0001-8590-3070; Burhan, Hakan/0000-0002-2293-7369Recently, the pyridazine nucleus has been widely studied in the field of particular and new medicinal factors as drugs acting on the cardiovascular system. Additionally, a number of thienopyridazines have been claimed to possess interacting biological macromolecules and pharmacological activities such as NAD(P)H oxidase inhibitor, anticancer, and identified as a novel allosteric modulator of the adenosine A1 receptor. The literature survey demonstrates that coumarin, 1,2-pyrazole benzothiazole, and 1,3- thiazole scaffolds are the most versatile class of molecules. In this study, a series of substituted pyrazole[3,4-d]pyridazine derivatives (2a-n) were prepared, and their structures were characterized by Mass analysis, NMR, and FT-IR. These obtained pyrazole [3,4-d]pyridazine compounds were very good inhibitors of the carbonic anhydrase (hCA I and II) isoenzymes and acetylcholinesterase (AChE) with K-i values in the range of 9.03 +/- 3.81-55.42 +/- 14.77 nM for hCA I, 18.04 +/- 4.55-66.24 +/- 19.21 nM for hCA II, and 394.77 +/- 68.13-952.93 +/- 182.72 nM for AChE, respectively. The possible inhibition mechanism of the best-posed pyrazole[3,4-d]pyridazine and pyrazole-3-carboxylic acid derivatives and their interaction with catalytic active pocket residues were determined based on the calculations.eninfo:eu-repo/semantics/closedAccessCarbonic AnhydraseEnzyme InhibitionComputational StudiesMolecular DockingArticle92Q1Q131470200WOS:000489699400072