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Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/76025
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dc.creatorTaniris Cafiero Bragapt_BR
dc.creatorÂngelo de Fátimapt_BR
dc.creatorThamara Ferreira Silvapt_BR
dc.creatorThamilla Maria Silva Macielpt_BR
dc.creatorEdjan Carlos Dantas da Silvapt_BR
dc.creatorEdeildo Ferreira da Silva-Júniorpt_BR
dc.creatorLuzia Valentina Modolopt_BR
dc.creatorIsis Martins Figueiredopt_BR
dc.creatorJosué Carinhanha Caldas Santospt_BR
dc.creatorThiago Mendonça de Aquinopt_BR
dc.date.accessioned2024-09-09T17:31:09Z-
dc.date.available2024-09-09T17:31:09Z-
dc.date.issued2019-
dc.citation.volume43pt_BR
dc.citation.spage15187pt_BR
dc.citation.epage15200pt_BR
dc.identifier.doihttps://doi.org/10.1039/C9NJ03556Gpt_BR
dc.identifier.issn1369-9261pt_BR
dc.identifier.urihttp://hdl.handle.net/1843/76025-
dc.description.resumoTwenty-six Biginelli adducts were synthesized through an ionic liquid-assisted synthesis with up to 92% yield. Sixteen of these Biginelli adducts were then assayed to determine their antiureolytic activity against purified urease from jack beans. The substances BA7-S, BA9-S and BA11-S were shown to be as efficient inhibitors as hydroxyurea, a positive control used in in vitro screening assay against urease. Fluorescence studies revealed that BA7-S, BA9-S, BA11-S and BA5-S possessed high binding constant values of 5.95, 6.72, 4.55, and 4.28 M−1, respectively, while BAS12-S, without substituents, showed a low value of log Kb = 2.16 M−1. In addition, in the most thermodynamically favorable BA5-S and BA7-S urease complexes, the corresponding Biginelli adducts were capable of interacting with the active site of urease through non-ionic interactions, such as hydrophobic interactions, or hydrogen and van der Waals interactions, respectively. In silico studies also supported that the BAs interact with the active site, confirming the fluorescence and kinetic assay studies, which clearly indicate that BA5-S and BA7-S are competitive inhibitors (Ki = 0.96 and 0.57 mM, respectively). In silico studies also showed that the substituents in the aromatic ring interact with Ni atoms to form a stable complex.pt_BR
dc.languageengpt_BR
dc.publisherUniversidade Federal de Minas Geraispt_BR
dc.publisher.countryBrasilpt_BR
dc.publisher.departmentICB - DEPARTAMENTO DE BOTÂNICApt_BR
dc.publisher.departmentICX - DEPARTAMENTO DE QUÍMICApt_BR
dc.publisher.initialsUFMGpt_BR
dc.relation.ispartofNew Journal of Chemistrypt_BR
dc.rightsAcesso Restritopt_BR
dc.subjectInibidores de ureasept_BR
dc.subjectAdutos de Biginellipt_BR
dc.subjectUrease inhibitionpt_BR
dc.subjectBiginelli adductspt_BR
dc.subjectIonic liquid-assistedpt_BR
dc.subjectAntiureolytic activitypt_BR
dc.subject.otherQuímicapt_BR
dc.subject.otherUrease - Inibidorespt_BR
dc.subject.otherFluorescênciapt_BR
dc.titleIonic liquid-assisted synthesis of dihydropyrimidin(thi)ones biginelli adducts and investigation of their mechanism of urease inhibitionpt_BR
dc.typeArtigo de Periódicopt_BR
dc.url.externahttps://pubs.rsc.org/en/content/articlelanding/2019/nj/c9nj03556g#!pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-8033-0434pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-4032-0100pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0003-2344-5590pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-6675-0301pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-1527-4501pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-1873-5342pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-9525-5123pt_BR
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