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• W4285676824 abstract "In this research, a series of N-phenylsulfonamide derivatives (1-12) were designed, synthesized, and investigated for their inhibitory potencies against carbonic anhydrase isoenzymes I, II, and IX (hCA I, hCA II, and hCA IX) and cholinesterases (ChE), namely, acetylcholinesterase and butyrylcholinesterase. These compounds, whose inhibition potentials were evaluated for the first time, were characterized by spectroscopic techniques (1 H- and 13 C-NMR and FT-IR). CA isoenzyme inhibitors are significant therapeutic targets, especially owing to their preventive/activation potential in the therapy processes of some diseases such as cancer, osteoporosis, and glaucoma. On the other hand, Cholinesterase inhibitors are valuable molecules with biological importance that can be employed in the therapy process of Alzheimer's patients. The results showed that the tested molecules had enzyme inhibition activities ranging from 9.7 to 93.7 nM against these five metabolic enzymes. Among the tested molecules, the methoxy and the hydroxyl group-containing compounds 10, 11, and 12 exhibited more enzyme inhibition activities when compared to standard compounds acetazolamide, sulfapyridine, and sulfadiazine for CA isoenzymes and neostigmine for ChE, respectively. Of these three molecules, compound 12, which had a hydroxyl group in the para position in the aromatic ring, was determined to be the most active molecule against all enzymes. In silico work, molecular docking has also shown similar results and is consistent with the experimental data in the study. As a result, we can say that some of the tested molecules might be used as promising inhibitor candidates for further studies on this topic." @default.
• W4285676824 created "2022-07-17" @default.
• W4285676824 creator A5023522299 @default.
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• W4285676824 date "2022-08-03" @default.
• W4285676824 modified "2023-10-11" @default.
• W4285676824 title "Biological activity and molecular docking studies of some <i>N</i>‐phenylsulfonamides against cholinesterases and carbonic anhydrase isoenzymes" @default.
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• W4285676824 doi "https://doi.org/10.1002/jmr.2982" @default.
• W4285676824 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35842829" @default.
• W4285676824 hasPublicationYear "2022" @default.
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