Analysis of the interaction between [Ru(phenanthroline)3]2+ and bovine serum albumin


The interaction of compounds with potential use as pharmaceutical with a carrier protein as serum albumin is of great importance in their biodistribution. Albumin offers different sites for binding metallic compounds. Using a combination of spectropho-tometric and electrochemical techniques, the interaction between [Ru(phen)3]Cl2 (phen = phenantroline) and bovine serum albumin was evaluated. In particular, it was possible to calculate an apparent binding constant (Kb) of 4.4 × 103 (for concentrations expressed in M) for the main interaction site of the protein. A number of ca. 40 molecules of Ru-phen per molecule of BSA under saturation conditions, and a positive cooperative behavior towards association from the protein were found.

Share and Cite:

Luzuriaga, L. and Cerdá, M. (2012) Analysis of the interaction between [Ru(phenanthroline)3]2+ and bovine serum albumin. Advances in Biological Chemistry, 2, 262-267. doi: 10.4236/abc.2012.23033.

Conflicts of Interest

The authors declare no conflicts of interest.


[1] Arjmand, F., Tewatia, P., Aziz, M. and Khan, R.H. (2009) Interaction studies of a novel Co(II)-based potential chemotherapeutic agent with human serum albumin (HSA) employing biophysical techniques. Medicinal Chemistry Research, 19, 794-807. doi:10.1007/s00044-009-9231-7
[2] Timerbaev, A.R., Hartinger, C.G., Aleksenko, S.S. and Keppler, B.K. (2006) Interactions of antitumor metallo-drugs with serum proteins: Advances in characterization using modern analytical methodology. Chemical Reviews, 106, 2224-2248. doi:10.1021/cr040704h
[3] Pyle, A.M., Rehmann, J.P., Meshoyrer, R., Kumar, C.V., Turro, N.J. and Barton, J.K. (1989) Mixed-ligand complexes of ruthenium(II): Factors governing binding to DNA. Journal of the American Chemical Society, 111, 3051-3058. doi:10.1021/ja00190a046
[4] Ravera, M., Gabano, E., Baracco, S., Sardi, M. and Osella, D. (2008) Electrochemical studies of a series of antimetastatic mono- and di-ruthenium complexes [Na] [trans-RuIIICl4(DMSO)(L)] and [Na]2[{trans-RuIIICl4 (DMSO)}2(μ-L)] (L=N-donor heterocyclic bridging lig- and). Inorganica Chimica Acta, 361, 2879-2886. doi:10.1016/j.ica.2008.02.031
[5] Zhang, Y.-Z., Li, H.-R., Dai, J., Chen, W.-J., Zhang, J. and Liu, Y. (2010) Spectroscopic studies on the binding of cobalt(II) 1,10-phenanthtoline complex to bovine serum albumin. Biological Trace Element Research, 135, 136-152. doi:10.1007/s12011-009-8502-y
[6] Kandagal, P.B., Ashoka, S., Seetharamappa, J., Shaikh, S.M.T., Jadegoud, Y. and Ijare, O.B. (2006) Study of the interaction of an anticancer drug with human and bovine serum albumin: Spectroscopic approach. Journal of Pharmaceutical and Biomedical Analysis, 41, 393-399. doi:10.1016/j.jpba.2005.11.037
[7] Ni, Y., Zhang, X. and Kokot, S. (2009) Spectrometric and voltammetric studies of the interaction between quercetin and bovine serum albumin using warfarin as site marker with the aid of chemometrics. Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 71, 1865- 1872. doi:10.1016/j.saa.2008.07.004
[8] Rahman, A.A. and Sharker, S.M. (2009) Determination of the binding sites of propranolol HCl on bovine serum albumin by direct and reverse procedures. Saudi Pharmaceutical Journal, 17, 249-253. doi:10.1016/j.jsps.2009.08.002
[9] Barton, J.K., Danishefsky, A.T. and Goldberg, J.M. (1984) Tris(phenanthroline)ruthenium(II): Stereoselectivity in binding to DNA. Journal of the American Chemical Society, 106, 2172-2176. doi:10.1021/ja00319a043
[10] Peters, T. (1996) All about albumin. Academic Press, New York.
[11] Creery, R.L.M. and Wieckowski, A. (1999) Interfacial electrochemistry. Marcel Dekker, New York.
[12] Efthimiadou, E.K., Karaliota, A. and Psomas, G. (2010) Metal complexes of the third-generation quinolone antimicrobial drug sparfloxacin: Structure and biological evaluation. Journal of Inorganic Biochemistry, 104, 455- 466. doi:10.1016/j.jinorgbio.2009.12.019
[13] Wolfe, A., G.H.S. Jr., and T. Meehan, (1987) Polycyclic aromatic hydrocarbons physically intercalate into duplex regions of denatured DNA. Biochemistry, 26, 6392-6396. doi:10.1021/bi00394a013
[14] Zeman, S.M., Depew, K.M., Danishefsky, S.J. and Crothers, D.M. (1998) Simultaneous determination of helical unwinding angles and intrinsic association constants in ligand-DNA complexes: The interaction between DNA and calichearubicin B. Proceedings of the National Academy of Sciences of the United States of America, 95, 4327-4332. doi:10.1073/pnas.95.8.4327
[15] Cerdá, M.F., Méndez, E., Obal, G., Kremer, C., Gancheff, J.S. and Luna, A.M.C. (2004) Voltammetric studies of the interaction between Re(V) complexes and proteins. Journal of Inorganic Biochemistry, 98, 238-244. doi:10.1016/j.jinorgbio.2003.08.013
[16] Leskovac, V. (2004) Comprehensive enzyme kinetics. Kluwer Academic, Plenum Publishers, New York.

Copyright © 2023 by authors and Scientific Research Publishing Inc.

Creative Commons License

This work and the related PDF file are licensed under a Creative Commons Attribution 4.0 International License.