Protein Binding of Biphenylylacetic Acid Derivatives

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Abstract
Protein binding of 4''-chloro-5-methoxy-3-biphenylylacetic acid (DKA-9), a newly developed anti-inflammatory agent, and its metabolites was examined using the equilibrium dialysis method. Scatchard plot data showed that they were bound strongly to bovine serum albumin and had 2 or more binding sites on the albumin molecule. The binding parameters were K1 = 2 .times. 104 M-1, K2 = 8 .times. 102 M-1, n1 = 11.5, n2 = 27.1 and these values were comparable with K1 of salicylic acid and quinidine, and of K1 .times. n1 of phenylbutazone. In order to obtain a clue to the understanding of the species differences, the binding behavior of DKA-9 to various animal [rabbit, rat, dog, monkey, human] plasma was also investigated. The binding parameters were obtained from the modified Scatchard plot analysis and there were considerable species differences. Apparently there was also a correlation between the species difference in protein binding and that in drug elimination rate.

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