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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

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

  AUTHORS: Laura Luzuriaga, María Fernanda Cerdá

  KEYWORDS: Saturation Graph; Spectrophotometry; Cyclic Voltammetry

  JOURNAL NAME: Advances in Biological Chemistry, Vol.2 No.3, August 22, 2012

  ABSTRACT: 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.