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Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/78030
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dc.creatorCamila P. Pereirapt_BR
dc.creatorLuzia Valentina Modolopt_BR
dc.creatorJosué Carinhanha Caldas Santospt_BR
dc.creatorÂngelo de Fátimapt_BR
dc.creatorAna Carolina Fradique de Lyrapt_BR
dc.creatorBreno Germano de Freitas Oliveirapt_BR
dc.creatorIgor José dos Santos Nascimentopt_BR
dc.creatorEdeildo Ferreira da Silva-Júniorpt_BR
dc.creatorThiago Mendonça de Aquinopt_BR
dc.creatorFrancesca Sistopt_BR
dc.creatorIsis Martins Figueiredopt_BR
dc.creatorFelipe Terra Martinspt_BR
dc.date.accessioned2024-11-13T21:03:52Z-
dc.date.available2024-11-13T21:03:52Z-
dc.date.issued2022-
dc.citation.volume33pt_BR
dc.citation.issue9pt_BR
dc.citation.spage1041pt_BR
dc.citation.epage1057pt_BR
dc.identifier.doihttps://dx.doi.org/10.21577/0103-5053.20220020pt_BR
dc.identifier.issn0103-5053pt_BR
dc.identifier.urihttp://hdl.handle.net/1843/78030-
dc.description.resumoIn this study, the interaction between benzothiazole (BTA, concentration of a drug required for 50% inhibition in vitro (IC 50) = 0.77 mM) and benzimidazole (BIA, IC 50 = 2.14 mM) with urease was quantitatively assessed, using UV-Vis, molecular fluorescence, and circular dichroism. The results showed that both compounds interact with urease by a static fluorescence quenching mechanism with a non-fluorescent complex formation. The main forces responsible for stabilizing the supramolecular complex between BTA and urease were hydrophobic while, for BIA, van der Waals interactions and hydrogen bonds were the main ones. Urease conformation changes due to the interaction process were analyzed by circular dichroism and synchronous fluorescence. Besides, a competitive assay with substrate and inhibitors was used to evaluate the preferential urease site of interaction with BTA and BIA. Our experimental and theoretical studies supported that both, BTA and BIA, are mixed-inhibitors of ureases with a slight preference to the active site of such enzymes. Finally, both BTA and BIA showed to possess anti-Helicobacter pylori (one reference strain and six clinical isolates) activity, presenting minimal inhibitory concentration (MIC) values ranging from 38-150 and 20-164 μM, respectively. The urease inhibitors omeprazole and hydroxyurea showed MIC values in the range of 46-185 μM and 1683-> 3366 μM, respectively.pt_BR
dc.description.sponsorshipCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológicopt_BR
dc.description.sponsorshipFAPEMIG - Fundação de Amparo à Pesquisa do Estado de Minas Geraispt_BR
dc.description.sponsorshipCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superiorpt_BR
dc.description.sponsorshipOutra Agênciapt_BR
dc.format.mimetypepdfpt_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.ispartofJournal of the Brazilian Chemical Societypt_BR
dc.rightsAcesso Abertopt_BR
dc.subjectUreasept_BR
dc.subjectUrease inhibitorpt_BR
dc.subjectBenzothiazolept_BR
dc.subjectBenzimidazolept_BR
dc.subjectDrug-protein interactionpt_BR
dc.subjectSpectroscopic techniquespt_BR
dc.subject.otherUrease - Inibidorespt_BR
dc.subject.otherBenzimidazoispt_BR
dc.subject.otherHelicobacter pyloript_BR
dc.subject.otherEnzimaspt_BR
dc.title2-(pyridin-4yl)benzothiazole and its benzimidazole-analogue: biophysical and in silico studies on their interaction with urease and in vitro anti-Helicobacter pylori activitiespt_BR
dc.typeArtigo de Periódicopt_BR
dc.url.externahttps://jbcs.sbq.org.br/default.asp?ed=330pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-8033-0434pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-9525-5123pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0003-2344-5590pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-5497-6912pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-2664-4336pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-1527-4501pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-9138-8466pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0003-0166-2164pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-1873-5342pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-9004-0927pt_BR
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