Abstract

NMR diffusion and relaxation measurements were applied to study the ibuprofen-protein interaction by changing the drug concentration in solutions containing 0.1 M human serum albumin (HSA). On the basis of the assumption that the drug molecules undergo fast exchange between the binding and free states, the association constant, Ka, for drug-HSA complexes is found to be about 60, and the number of binding sites, n, is about 50. The small association constant and the big binding site number suggest weak interactions between ibuprofen and HAS.

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