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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)3Cl2 (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.
Luzuriaga et al. (Sun,) studied this question.