Table of Contents
Metal-Based Drugs
Volume 7, Issue 6, Pages 335-342

Binding of Antitumor Ruthenium(III) Complexes to Plasma Proteins

1Department of Chemtstry, University of Florence, Via Capponi 7, Florence I-50121, Italy
2Department of Inorganic Chemistry, University of Sevilla, Aptdo. 553, Sevilla 41071, Spain
3Department of Chemical Sciences, University of Trieste, Via Giorgeri 1, Trieste 34127, Italy
4Institute of Inorganic Chemistry, University of Vienna, Wahringerstrasse 42, Wien A-1090, Austria

Received 11 January 2001; Accepted 21 January 2001

Copyright © 2000 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Presently, there is large interest in analysing the interactions in vitro with plasma proteins of some novel antitumor ruthenium(III) complexes that are in preclinical or clinical phase. The joint application of separation and spectroscopic techniques provides valuable information on the nature and the properties of the resulting ruthenium/protein adducts. Recent work carried out in our laboratory points out that, under physiological conditions, some selected ruthenium(III) complexes bind plasma proteins tightly with a marked preference for surface imidazole groups. Representative examples of interactions of antitumor ruthenium(III) complexes with plasma proteins such as albumin and transferrin are given. Notably the antitumor ruthenium(III) complexes considered here bind proteins much tighter than DNA; it is proposed that protein binding of ruthenium(III) complexes will have a large impact on the biodistribution, the pharmacokinetics and the mechanism of action of these experimental drugs.