Analysis of the interaction between [Ru(phenanthroline)3]2+ and bovine serum albumin英文文献资料.docVIP

Advances in Biological Chemistry, 2012, 2, 262-267 ABC /10.4236/abc.2012.23033 Published Online August 2012 (http://www.SciRP.org/journal/abc/) Analysis of the interaction between [Ru(phenanthroline)3]2+ and bovine serum albumin Laura Luzuriaga, María Fernanda Cerdá * Laboratorio de Biomateriales, Facultad de Ciencias, Montevideo, Uruguay * Email: fcerda@.uy Received 17 April 2012; revised 18 May 2012; accepted 27 May 2012 ABSTRACT Medicine with proteins should be an important charac- terization step, because the union with serum proteins like albumin has a great influence in the way the com- pound is distributed in vivo. Nevertheless, studies of this type are scarce in the literature, and different techniques have been reported with this aim [5-9]. Among them, fluorescence spectroscopy, gel chromatography, dialysis, ultra filtration, NMR and HPLC are among the most used. The goal of this work was to characterize the union The interaction of compounds with potential use as pharmaceutical with a carrier protein as serum al- bumin is of great importance in their biodistribution. Albumin offers different sites for binding metallic com- pounds. Using a combination of spectrophotometric and electrochemical techniques, the interaction be- tween [Ru(phen)3]Cl2 (phen = phenantroline) and bo- vine serum albumin was evaluated. In particular, it was possible to calculate an apparent binding constant between [Ru(phenanthroline)3] 2+ (phenanthroline = phen) and bovine serum albumin (BSA) using cyclic voltam- metry and UV-visible measurements. BSA was used be- cause it is structurally very similar to the human serum albumin [10], but with a lower price and a higher purity. (Kb) of 4.4 × 10 (for concentrations expressed in M) 3 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 coopera- tiv