Pyrazole[3,4-d]pyridazine derivatives: Molecular docking and explore of acetylcholinesterase and carbonic anhydrase enzymes inhibitors as anticholinergics potentials.

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ID: 43611
2019
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Abstract
Recently, 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 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.
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taslimi2019pyrazole34dpyridazinebioorganic Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Taslimi, Parham;Türkan, Fikret;Cetin, Adnan;Burhan, Hakan;Karaman, Muhammet;Bildirici, Ishak;Gulçin, İlhami;Şen, Fatih;
Journal Bioorganic chemistry
Year 2019
DOI
S0045-2068(19)30476-6
URL
Keywords
molecular docking enzyme inhibition carbonic anhydrase computational studies

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