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|Title:||Drug-protein recognition processes investigated by NMR relaxation data. A study on corticosteroid-albumin interactions||Authors:||Martini, S
|Issue Date:||2006||Project:||None||Journal:||BIOCHEMICAL PHARMACOLOGY||Abstract:||
In this paper we investigated the interaction processes occurring at the protein–solventinterface for prednisolone–albumin and prednisone–albumin systems, using an approachbased on the analysis of proton selective relaxation rate enhancements of the ligand in thepresence of the macromolecule. The contribution from the bound ligand fraction to theobserved relaxation rate in relation to protein concentration allowed the calculation of theaffinity index ½ATL and the normalized affinity index ½ANITL which removes the effects of motionalanisotropies and different proton densities, and isolates the contribution due to a decreasein the ligand dynamics caused by the binding with the protein. This approach allowed thecomparison of the binding ability of prednisolone and prednisone towards albumin.
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