Thimerosal changes protein conformation and increase the rate of fibrillation in physiological conditions: spectroscopic studies using bovine serum albumin (bsa)

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dc.creatorJoão César Nascimento Santos
dc.creatorIsabella Miranda da Silva
dc.creatorTaniris Cafiero Braga
dc.creatorÂngelo de Fátima
dc.creatorIsis Martins Figueiredo
dc.creatorJosué Carinhanha Caldas Santos
dc.date.accessioned2024-09-23T20:48:22Z
dc.date.accessioned2025-09-08T23:59:30Z
dc.date.available2024-09-23T20:48:22Z
dc.date.issued2018
dc.description.sponsorshipCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológico
dc.description.sponsorshipCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
dc.description.sponsorshipOutra Agência
dc.format.mimetypepdf
dc.identifier.doihttps://doi.org/10.1016/j.ijbiomac.2018.02.116
dc.identifier.issn0141-8130
dc.identifier.urihttps://hdl.handle.net/1843/76835
dc.languageeng
dc.publisherUniversidade Federal de Minas Gerais
dc.relation.ispartofInternational Journal of Biological Macromolecules
dc.rightsAcesso Aberto
dc.subjectCompostos orgânicos
dc.subjectSoros
dc.subjectAlbumina
dc.subjectAnálise espectral
dc.subject.otherThimerosal
dc.subject.otherBSA and ethylmercury
dc.subject.otherProtein fibrillation
dc.subject.otherInteraction mechanism
dc.titleThimerosal changes protein conformation and increase the rate of fibrillation in physiological conditions: spectroscopic studies using bovine serum albumin (bsa)
dc.typeArtigo de periódico
local.citation.epage1040
local.citation.spage1032
local.citation.volume113
local.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.
local.identifier.orcidhttps://orcid.org/0000-0002-4032-0100
local.identifier.orcidhttps://orcid.org/0000-0003-2344-5590
local.identifier.orcidhttps://orcid.org/0000-0002-1873-5342
local.identifier.orcidhttps://orcid.org/0000-0002-9525-5123
local.publisher.countryBrasil
local.publisher.departmentICX - DEPARTAMENTO DE QUÍMICA
local.publisher.initialsUFMG
local.url.externahttps://www.sciencedirect.com/science/article/pii/S0141813018302009

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