Abstract
A new method to determine the interaction between drug and protein has been developed by utilizing the technique of microdialysis sampling with the ketoprofen and the human serum albumin (HSA) as the model of drug and protein. Two kinds of binding sites of HSA to ketoprofen have been observed. The binding constants and number of binding sites obtained by the Scatchard equation are 0.799, 3.18×lo6 mol-1 ·L and 2.15, 2.01×105 mol-1 ·L, respectively. The displacement binding of drugs to HSA has also been studied. The strong displacement of competitive binding of ibuprofen with ketoprofen to HSA was observed, which means that the primary binding site of HSA to ketoprofen and that to ibuprofen are the same. However, only a weaker displacement of warfarin for the association of ketoprofen with HSA was observed, which may suggest that the primary binding site of HSA to ketoprofen is different from that to warfarin. Such a displacement effect for competitive binding of drugs to HSA was explained by the displacement model in the liquid-solid adsorption chromatography.
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