Table of Contents
Metal-Based Drugs
Volume 7, Issue 6, Pages 293-299

Interaction of Cis- and Trans-RuCl2(DMSO)4 With Human Serum Albumin

1Faculty of Chemistry, University of Wroclaw, F.Joliot Curie 14, Wroclaw 50-383, Poland
2NCRS ‘DEMOKRITOS’, Athens, Greece

Received 28 June 2000; Accepted 3 August 2000

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.


The interaction between cis- and trans- RuCl2(DMSO)4 and human serum albumin have been investigated through UV-Vis, circular dichroism, fluorescence spectroscopy and inductively couplet plasma atomic emission spectroscopy (ICP(AES)) method Albumin can specifically bind 1 mole of cis-isomer and 2 moles of the trans-isomer RuCl2(DMSO)4 complex. The interaction of RuCl2(DMSO)4 with HSA causes: a conformational change with the loss of helical stability of protein; the strong quenching of the Trp 214 fluorescence indicating that the conformational change of the hydrophobic binding pocked in subdomain IIA takes place; a local perturbation of the warfarin binding site and induce some conformational changes at neighbour domains, a changing of the binding abilities towards heme.