Peculiar reactivity of a di-imine copper(ii) complex regarding its binding to albumin protein
| Autor: | Maurício Cavicchioli, Marcos Brown Gonçalves, Helena M. Petrilli, Ana Maria da Costa Ferreira, David E. P. Fonseca, Leandro de Rezende, Vivian Chagas da Silveira, Antonia Tavares do Amaral, Giovanni F. Caramori, Mariana Pedrinha Abbott |
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| Rok vydání: | 2013 |
| Předmět: |
Models
Molecular Pyrazine Pyridines Stereochemistry Imine Molecular Conformation chemistry.chemical_element Metal Binding Site Ligands law.invention Inorganic Chemistry chemistry.chemical_compound law Pyridine Organometallic Compounds Animals Humans Imidazole Electron paramagnetic resonance Serum Albumin COBRE Ligand Imidazoles Copper Crystallography chemistry Pyrazines Cattle Imines Reactive Oxygen Species Protein Binding |
| Zdroj: | Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP |
| ISSN: | 1477-9234 1477-9226 |
| DOI: | 10.1039/c3dt00108c |
| Popis: | A set of four di-imine copper(II) complexes containing pyridine, pyrazine and/or imidazole moieties, [Cu(apyhist)H2O](2+) 1 (apyhist = 2-(1H-imidazol-4-yl)-N-(1-(pyridin-2-yl)ethylidene)ethanamine), [Cu(apzhist)OH](+) 2 (apzhist = 2-(1H-imidazol-4-yl)-N-(1-(pyrazin-2-yl)ethylidene)ethanamine), [Cu(apyepy)OH](+) 3 (apyepy = 2-(pyridin-2-yl)-N-(1-(pyridin-2-yl)ethylidene)ethanamine), and [Cu(apzepy)H2O](2+) 4 (apzepy = N-(1-(pyrazin-2-yl)ethylidene)-2-(pyridin-2-yl)ethanamine), were investigated regarding their capability of interacting with serum albumin (human, HSA and bovine, BSA), by using spectroscopic techniques, CD, UV/Vis and EPR. Like other similar di-imine copper(II) complexes, most of them showed an expected preferential insertion of the metal ion at the primary N-terminal site of the protein, very selective for copper and characterized by a CD band at 560 nm. Further insertion of the copper ion at a secondary site is expected when using an excess of the metal. However, one of these studied complexes, [Cu(apyhist)H2O](2+) 1, exhibited anomalous behaviour interacting only at this secondary metal binding site of albumin, characterized by a CD band at 370 nm, and attributed to the coordination of copper at the Cys34 pocket. Analogous experiments with HSA previously treated with N-ethyl-maleimide (NEM), that oxidizes the protein Cys34 residue and obstructs the metal coordination, verified these results. Additional data obtained by EPR spectroscopy complemented those results. DFT calculations, considering some structural and electronic characteristics of such series of di-imine ligands and of the corresponding copper complexes, suggested molecular recognition of the apyhist ligand at the protein cavity as a feasible explanation for this unexpected and peculiar behaviour of complex 1. |
| Databáze: | OpenAIRE |
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