Journal
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
Volume 18, Issue 1, Pages 9-17Publisher
SPRINGER
DOI: 10.1007/s00775-012-0944-6
Keywords
Solution equilibrium; Albumin; Binding affinity; Fluorescence; Ruthenium anticancer agents; Site markers
Funding
- Hungarian Research Foundation OTKA [K77833, TAMOP-4.2.1/B-09/1/KONV-2010-0005]
- European Regional Fund
- J. Bolyai Research Fellowship
- Austrian Science Fund (FWF) [I496-B11]
- COST [D39, CM0902]
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Indazolium trans-[tetrachloridobis(1H-indazole)ruthenate(III)] (KP1019) and its Na+ analogue (KP1339) are two of the most prominent non-platinum antitumor metal complexes currently undergoing clinical trials. After intravenous administration, they are known to bind to human serum albumin (HSA) in a noncovalent manner. To elucidate their HSA binding sites, displacement reactions with the established site markers warfarin and dansylglycine as well as bilirubin were monitored by spectrofluorimetry, ultrafiltration-UV-vis spectrophotometry, and/or capillary zone electrophoresis. Conditional stability constants for the binding of KP1019 and KP1339 to sites I and II of HSA were determined, indicating that both Ru(III) compounds bind to both sites with moderately strong affinity (log K (1)' = 5.3-5.8). No preference for either binding site was found, and similar results were obtained for both metal complexes, demonstrating low influence of the counter ion on the binding event.
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