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Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/76835
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dc.creatorJoão César Nascimento Santospt_BR
dc.creatorIsabella Miranda da Silvapt_BR
dc.creatorTaniris Cafiero Bragapt_BR
dc.creatorÂngelo de Fátimapt_BR
dc.creatorIsis Martins Figueiredopt_BR
dc.creatorJosué Carinhanha Caldas Santospt_BR
dc.date.accessioned2024-09-23T20:48:22Z-
dc.date.available2024-09-23T20:48:22Z-
dc.date.issued2018-
dc.citation.volume113pt_BR
dc.citation.spage1032pt_BR
dc.citation.epage1040pt_BR
dc.identifier.doihttps://doi.org/10.1016/j.ijbiomac.2018.02.116pt_BR
dc.identifier.issn0141-8130pt_BR
dc.identifier.urihttp://hdl.handle.net/1843/76835-
dc.description.resumoThe interaction between bovine serum albumin (BSA) and thimerosal (TM), an organomercury compound widely employed as a preservative in vaccines, was investigated simulating physiological conditions and using different spectroscopic techniques. The results, employing molecular fluorescence showed the interaction occurs by static quenching through electrostatic forces (ΔH < 0 and ΔS > 0), spontaneously (ΔG = −4.40 kJ mol−1) and with a binding constant of 3.24 × 103 M−1. Three-dimensional fluorescence studies indicated that TM causes structural changes in the polypeptide chain of the BSA, confirmed by circular dichroism that showed an increase in α-helix (from 43.9 to 47.8%) content after interaction process. Through synchronized fluorescence and employing bilirubin as a protein site marker, it was confirmed the preferential interaction of TM in the subdomain IB of BSA. The interaction mechanism proposed in this work is based on the reaction of TM with BSA through of free Cys34 residue, forming the adduct BSA-HgEt with the thiosalicylic acid release, which possibly interacts electrostatically with positive side chain amino acids of the modified protein. Finally, it was proven that both TM and EtHgCl accelerate the protein fibrillation kinetics in 42 and 122%, respectively, indicating the toxicity of these compounds in biological systems.pt_BR
dc.description.sponsorshipCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológicopt_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.departmentICX - DEPARTAMENTO DE QUÍMICApt_BR
dc.publisher.initialsUFMGpt_BR
dc.relation.ispartofInternational Journal of Biological Macromoleculespt_BR
dc.rightsAcesso Abertopt_BR
dc.subjectThimerosalpt_BR
dc.subjectBSA and ethylmercurypt_BR
dc.subjectProtein fibrillationpt_BR
dc.subjectInteraction mechanismpt_BR
dc.subject.otherCompostos orgânicospt_BR
dc.subject.otherSorospt_BR
dc.subject.otherAlbuminapt_BR
dc.subject.otherAnálise espectralpt_BR
dc.titleThimerosal changes protein conformation and increase the rate of fibrillation in physiological conditions: spectroscopic studies using bovine serum albumin (bsa)pt_BR
dc.typeArtigo de Periódicopt_BR
dc.url.externahttps://www.sciencedirect.com/science/article/pii/S0141813018302009pt_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/0000-0002-1873-5342pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-9525-5123pt_BR
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