Synthesis and human carbonic anhydrase I, II, VA, and XII inhibition with novel amino acid-sulphonamide conjugates

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dc.authoridKUCUKBAY, HASAN/0000-0002-7180-9486
dc.authoridKucukbay, Fatumetuzzehra/0000-0001-7784-4138
dc.authoridBugday, Nesrin/0000-0002-3882-035X
dc.authoridBartolucci, Gianluca/0000-0002-5631-8769
dc.authoridangeli, andrea/0000-0002-1470-7192
dc.authoridSupuran, Claudiu/0000-0003-4262-0323
dc.authoridReis, AlessanRSS/0000-0001-8486-7469
dc.authorwosidKUCUKBAY, HASAN/A-5050-2019
dc.contributor.authorKucukbay, Hasan
dc.contributor.authorBugday, Nesrin
dc.contributor.authorKucukbay, F. Zehra
dc.contributor.authorAgeli, Andrea
dc.contributor.authorBartolucci, Gianluca
dc.contributor.authorSupuran, Claudiu T.
dc.date.accessioned2024-08-04T20:47:04Z
dc.date.available2024-08-04T20:47:04Z
dc.date.issued2020
dc.departmentİnönü Üniversitesien_US
dc.description.abstractA series of amino acid-sulphonamide conjugates was prepared through benzotriazole mediated coupling reactions and characterised by H-1-NMR, C-13-NMR, MS, and FTIR spectroscopic techniques as well as elemental analysis. The carbonic anhydrase (CA, EC 4.2.1.1) inhibitory activity of the new compounds was determined against four human (h) isoforms, hCA I, hCA II, hCA VA, and hCA XII. Most of the synthesised compounds showed effective in vitro CA inhibitory properties. The new amino acid-sulphonamide conjugates showed potent inhibitory activity against hCA II, some of them at subnanomolar levels, exhibiting more effective inhibitory activity compared to the standard drug acetazolamide. Some of these sulphonamides were also found to be effective inhibitors of hCA I, hCA VA, and hCA XII, with activity from the low to high nanomolar range.en_US
dc.description.sponsorshipInonu University, Turkey [FDP-2018-1352, FUA-2018-1106, FUA-2018-1101]; Universita degli Studi di Firenze, Italyen_US
dc.description.sponsorshipWe thank Inonu University, Turkey [BAPB-Grand No: FDP-2018-1352, FUA-2018-1106, and FUA-2018-1101], Universita degli Studi di Firenze, Italy for financial support.en_US
dc.identifier.doi10.1080/14756366.2019.1710503
dc.identifier.endpage497en_US
dc.identifier.issn1475-6366
dc.identifier.issn1475-6374
dc.identifier.issue1en_US
dc.identifier.pmid31914827en_US
dc.identifier.scopus2-s2.0-85077612433en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage489en_US
dc.identifier.urihttps://doi.org/10.1080/14756366.2019.1710503
dc.identifier.urihttps://hdl.handle.net/11616/99137
dc.identifier.volume35en_US
dc.identifier.wosWOS:000506434800001en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherTaylor & Francis Ltden_US
dc.relation.ispartofJournal of Enzyme Inhibition and Medicinal Chemistryen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectCarbonic anhydraseen_US
dc.subjectinhibitoren_US
dc.subjectsulphonamideen_US
dc.subjectamino aciden_US
dc.subjectconjugateen_US
dc.titleSynthesis and human carbonic anhydrase I, II, VA, and XII inhibition with novel amino acid-sulphonamide conjugatesen_US
dc.typeArticleen_US

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