Abstract
The effect of acetonitrile (ACN) on the low-affinity interaction between human serum albumin (HSA) and ibuprofen (IBP) was studied using 1H-NMR techniques. Both chemical shift and relaxation measurements showed the addition of ACN to the solutions decreased the binding affinity of IBP to HSA and reduced the hydrophobic interaction between them. The self-diffusion coefficients of IBP were measured as a function of the drug concentration at different ACN concentrations. The association constant, K a, for ligand–HSA complexes and the number of binding sites, n, are evaluated by the application of Langmuir isotherm. The results indicated that the value of n was about 38 without ACN, and about 26 with ACN concentration 12% (v/v%). The decreased binding capacity of IBP to HSA in the presence of ACN was mainly attributed to the competition of ACN with IBP to the low-affinity binding sites of HSA molecule.
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