aDepartment of Chemical and Biosystem Sciences, University of Siena, Via Aldo Moro 2, 53100 Siena, ItalybDepartment of Pharmaceutical Chemistry, University of Siena, Via Aldo Moro 2, 53100 Siena, ItalycPolo Universitario Colle di Val d'Elsa, University of Siena, Viale Matteotti 15, 53034 Colle di Val d'Elsa (SI), Siena, Italy
Checking for direct PDF access through Ovid
In this paper we investigated the interaction processes occurring at the protein-solvent interface for prednisolone-albumin and prednisone-albumin systems, using an approach based on the analysis of proton selective relaxation rate enhancements of the ligand in the presence of the macromolecule. The contribution from the bound ligand fraction to the observed relaxation rate in relation to protein concentration allowed the calculation of the affinity indexSymbol and the normalized affinity indexSymbol which removes the effects of motional anisotropies and different proton densities, and isolates the contribution due to a decrease in the ligand dynamics caused by the binding with the protein. This approach allowed the comparison of the binding ability of prednisolone and prednisone towards albumin.