Metal-Based Drugs 
Volume 7 (2000), Issue 6, Pages 293-299
doi:10.1155/MBD.2000.293

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

Lilianna Trynda-Lemiesz,1 Henryk Kozlowski,1 and Nikolas Katsaros2

 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

Abstract

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.