Article citationsMore>>

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

has been cited by the following article:

• 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.