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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
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]
Total Authors: 7
Affiliation:
[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
Total Affiliations: 4
Document type: Journal article
Source: Journal of Coordination Chemistry; v. 71, n. 11-13, SI, p. 1894-1909, 2018.
Web of Science Citations: 0
Abstract

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)

FAPESP's process: 11/50318-1 - Development of compounds with pharmacological or medicinal interest and of systems for their transport, detection and recognition in biological media
Grantee:Ana Maria da Costa Ferreira
Support type: Research Projects - Thematic Grants
FAPESP's process: 13/07937-8 - Redoxome - Redox Processes in Biomedicine
Grantee:Ohara Augusto
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC