Use este identificador para citar o ir al link de este elemento: http://hdl.handle.net/1843/76835
Tipo: Artigo de Periódico
Título: Thimerosal changes protein conformation and increase the rate of fibrillation in physiological conditions: spectroscopic studies using bovine serum albumin (bsa)
Autor(es): João César Nascimento Santos
Isabella Miranda da Silva
Taniris Cafiero Braga
Ângelo de Fátima
Isis Martins Figueiredo
Josué Carinhanha Caldas Santos
Resumen: The 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.
Asunto: Compostos orgânicos
Soros
Albumina
Análise espectral
Idioma: eng
País: Brasil
Editor: Universidade Federal de Minas Gerais
Sigla da Institución: UFMG
Departamento: ICX - DEPARTAMENTO DE QUÍMICA
Tipo de acceso: Acesso Aberto
Identificador DOI: https://doi.org/10.1016/j.ijbiomac.2018.02.116
URI: http://hdl.handle.net/1843/76835
Fecha del documento: 2018
metadata.dc.url.externa: https://www.sciencedirect.com/science/article/pii/S0141813018302009
metadata.dc.relation.ispartof: International Journal of Biological Macromolecules
Aparece en las colecciones:Artigo de Periódico

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