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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Binding affinity studies of 1,2,3-triazole copper(II) complexes to human serum albumin

Texto completo
Autor(es):
de Paula, Queite A. [1, 2] ; Joly, Jean-Pierre [3] ; Selmeczi, Katalin [3] ; Fonseca, David E. P. [4] ; Caramori, Giovanni F. [4] ; Farrell, Nicholas P. [2] ; Da Costa Ferreira, Ana M. [1]
Número total de Autores: 7
Afiliação do(s) autor(es):
[1] Univ Sao Paulo, Inst Quim, Dept Quim Fundamental, Av Prof Lineu Prestes 748, BR-05508900 Sao Paulo - Brazil
[2] Virginia Commonwealth Univ, Dept Chem, Box 2006, Richmond, VA 23284 - USA
[3] Univ Lorraine, L2CM, UMR 7053, Fac Sci, CNRS, Vandoeuvre Les Nancy - France
[4] Univ Fed Santa Catarina, Dept Quim, Florianopolis, SC - Brazil
Número total de Afiliações: 4
Tipo de documento: Artigo Científico
Fonte: Journal of Coordination Chemistry; v. 71, n. 11-13, SI, p. 1894-1909, 2018.
Citações Web of Science: 0
Resumo

Two copper(II) complexes with tetradentate 1,4-disubstituted-1,2,3-triazole ligands, {[}CuL(MeCN)](ClO4)(2) (1) and {[}CuL](ClO4)(2) (2), have been prepared and characterized by different techniques, including X-ray structure determination, spectroscopic, and electrochemical measurements, as reported elsewhere. Herein, we report the interactions of these complexes, and corresponding free ligands, with human serum albumin (HSA) verifying their relative thermodynamic stability and differences in binding to this protein. Interactions with HSA were verified by CD measurements monitored at 564nm, up to stoichiometric ratio 2:1 {[}Complex]:{[}protein], according to competitive equilibria involving the insertion of copper at the selective N-terminal metal binding site in HSA, and additionally at a secondary nonselective site. Further interactions of these complexes with L-tryptophan residues, and probable supplementary site(s) for the binding, were followed by fluorescence measurements. Analogous experiments with the free L and L indicated much weaker interactions. Protein oxidation damage was observed for both complexes, monitored by carbonyl groups formation in the presence of H2O2, probably with the participation of reactive oxygen species. Density functional theory calculations exhibit metal-ligand binding interaction energies similar to {[}Cu(HSA-N-terminal)](+), and reinforced the experimental results, showing clearly that such triazole ligands are competitive toward copper(II) in biological medium. {[}GRAPHICS] . (AU)

Processo FAPESP: 11/50318-1 - Desenvolvimento de compostos com interesse farmacológico ou medicinal e de sistemas para seu transporte, detecção e reconhecimento no meio biológico
Beneficiário:Ana Maria da Costa Ferreira
Linha de fomento: Auxílio à Pesquisa - Temático
Processo FAPESP: 11/50204-6 - Espécies complexas de cobre e zinco com ligantes triazólicos: síntese, caracterização e estudo de atividade biológica
Beneficiário:Queite Antonia de Paula
Linha de fomento: Bolsas no Brasil - Pós-Doutorado
Processo FAPESP: 13/07937-8 - Redoxoma
Beneficiário:Ohara Augusto
Linha de fomento: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs