Toxicity of thimerosal in biological systems: Conformational changes in human hemoglobin, decrease of oxygen binding capacity, increase of protein glycation and amyloid's formation.

Autor: de Magalhães Silva M; Institute of Chemistry and Biotechnology, Federal University of Alagoas (UFAL), Campus A.C. Simões, 57072-900 Maceió, Alagoas, Brazil., de Araújo Dantas MD; Institute of Chemistry and Biotechnology, Federal University of Alagoas (UFAL), Campus A.C. Simões, 57072-900 Maceió, Alagoas, Brazil., da Silva Filho RC; Institute of Chemistry and Biotechnology, Federal University of Alagoas (UFAL), Campus A.C. Simões, 57072-900 Maceió, Alagoas, Brazil., Dos Santos Sales MV; Institute of Chemistry and Biotechnology, Federal University of Alagoas (UFAL), Campus A.C. Simões, 57072-900 Maceió, Alagoas, Brazil., de Almeida Xavier J; Institute of Chemistry and Biotechnology, Federal University of Alagoas (UFAL), Campus A.C. Simões, 57072-900 Maceió, Alagoas, Brazil., Leite ACR; Institute of Chemistry and Biotechnology, Federal University of Alagoas (UFAL), Campus A.C. Simões, 57072-900 Maceió, Alagoas, Brazil., Goulart MOF; Institute of Chemistry and Biotechnology, Federal University of Alagoas (UFAL), Campus A.C. Simões, 57072-900 Maceió, Alagoas, Brazil., Grillo LAM; Pharmacy Institute, Federal University of Alagoas (UFAL), Campus A.C. Simões, 57072-900 Maceió, Alagoas, Brazil., de Barros WA; Department of Chemistry, Federal University of Minas Gerais (UFMG), 31270-901 Belo Horizonte, Minas Gerais, Brazil., de Fátima Â; Department of Chemistry, Federal University of Minas Gerais (UFMG), 31270-901 Belo Horizonte, Minas Gerais, Brazil., Figueiredo IM; Institute of Chemistry and Biotechnology, Federal University of Alagoas (UFAL), Campus A.C. Simões, 57072-900 Maceió, Alagoas, Brazil., Santos JCC; Institute of Chemistry and Biotechnology, Federal University of Alagoas (UFAL), Campus A.C. Simões, 57072-900 Maceió, Alagoas, Brazil. Electronic address: josue@iqb.ufal.br.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2020 Jul 01; Vol. 154, pp. 661-671. Date of Electronic Publication: 2020 Mar 19.
DOI: 10.1016/j.ijbiomac.2020.03.156
Abstrakt: Thimerosal (TH), an organomercurial compound, is used as a preservative in vaccines and cosmetics. Its interaction with human hemoglobin (Hb) was investigated under physiological conditions using biophysical and biological assays, aiming to evaluate hazardous effects. TH interacts spontaneously with Hb (stoichiometry 2:1, ligand-protein), preferably by electrostatic forces, with a binding constant of 1.41 × 10 6  M -1 . Spectroscopic data allows to proposing that TH induces structural changes in Hg, through ethylmercury transfer to human Hb-Cys93 residues, forming thiosalicylic acid, which, in turn, interacts with the positive side of the amino acid in the Hb-HgEt adduct chain. As a consequence, inhibition of Hb-O 2 binding capacity up to 72% (human Hb), and 50% (human erythrocytes), was verified. Dose-dependent induction of TH forming advanced glycation end products (AGE) and protein aggregates (amyloids) was additionally observed. Finally, these results highlight the toxic potential of the use of TH in biological systems, with a consequent risk to human health.
Competing Interests: Declaration of competing interest The authors declare no competing or financial interests.
(Copyright © 2020 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE