Issue 46, 2014

Interactions of gold-based drugs with proteins: the structure and stability of the adduct formed in the reaction between lysozyme and the cytotoxic gold(iii) compound Auoxo3

Abstract

The structure and stability of the adduct formed in the reaction between Auoxo3, a dinuclear gold(III) compound, and the model protein hen egg white lysozyme (HEWL) are investigated by X-ray crystallography, UV-Vis absorption spectroscopy and circular dichroism (CD). It is found that Auoxo3 breaks down completely, undergoes reduction and produces reactive gold(I) species able to bind the protein and form stable derivatives. The behaviour of Auoxo3 is compared with that of two analogous gold(III) complexes previously studied: a few significant differences are highlighted. The general implications of these new results for the mode of action of cytotoxic gold complexes are discussed.

Graphical abstract: Interactions of gold-based drugs with proteins: the structure and stability of the adduct formed in the reaction between lysozyme and the cytotoxic gold(iii) compound Auoxo3

Supplementary files

Article information

Article type
Paper
Submitted
31 Jul 2014
Accepted
25 Sep 2014
First published
25 Sep 2014

Dalton Trans., 2014,43, 17483-17488

Interactions of gold-based drugs with proteins: the structure and stability of the adduct formed in the reaction between lysozyme and the cytotoxic gold(III) compound Auoxo3

I. Russo Krauss, L. Messori, M. A. Cinellu, D. Marasco, R. Sirignano and A. Merlino, Dalton Trans., 2014, 43, 17483 DOI: 10.1039/C4DT02332C

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