Ionic liquid-assisted synthesis of dihydropyrimidin(thi)ones biginelli adducts and investigation of their mechanism of urease inhibition

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dc.creatorTaniris Cafiero Braga
dc.creatorÂngelo de Fátima
dc.creatorThamara Ferreira Silva
dc.creatorThamilla Maria Silva Maciel
dc.creatorEdjan Carlos Dantas da Silva
dc.creatorEdeildo Ferreira da Silva-Júnior
dc.creatorLuzia Valentina Modolo
dc.creatorIsis Martins Figueiredo
dc.creatorJosué Carinhanha Caldas Santos
dc.creatorThiago Mendonça de Aquino
dc.date.accessioned2024-09-09T17:31:09Z
dc.date.accessioned2025-09-09T00:29:26Z
dc.date.available2024-09-09T17:31:09Z
dc.date.issued2019
dc.identifier.doihttps://doi.org/10.1039/C9NJ03556G
dc.identifier.issn1369-9261
dc.identifier.urihttps://hdl.handle.net/1843/76025
dc.languageeng
dc.publisherUniversidade Federal de Minas Gerais
dc.relation.ispartofNew Journal of Chemistry
dc.rightsAcesso Restrito
dc.subjectQuímica
dc.subjectUrease - Inibidores
dc.subjectFluorescência
dc.subject.otherInibidores de urease
dc.subject.otherAdutos de Biginelli
dc.subject.otherUrease inhibition
dc.subject.otherBiginelli adducts
dc.subject.otherIonic liquid-assisted
dc.subject.otherAntiureolytic activity
dc.titleIonic liquid-assisted synthesis of dihydropyrimidin(thi)ones biginelli adducts and investigation of their mechanism of urease inhibition
dc.typeArtigo de periódico
local.citation.epage15200
local.citation.spage15187
local.citation.volume43
local.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.
local.identifier.orcidhttps://orcid.org/0000-0002-8033-0434
local.identifier.orcidhttps://orcid.org/0000-0002-4032-0100
local.identifier.orcidhttps://orcid.org/0000-0003-2344-5590
local.identifier.orcidhttps://orcid.org/0000-0002-6675-0301
local.identifier.orcidhttps://orcid.org/0000-0002-1527-4501
local.identifier.orcidhttps://orcid.org/0000-0002-1873-5342
local.identifier.orcidhttps://orcid.org/0000-0002-9525-5123
local.publisher.countryBrasil
local.publisher.departmentICB - DEPARTAMENTO DE BOTÂNICA
local.publisher.departmentICX - DEPARTAMENTO DE QUÍMICA
local.publisher.initialsUFMG
local.url.externahttps://pubs.rsc.org/en/content/articlelanding/2019/nj/c9nj03556g#!

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