Binding of Coumarin Anticoagulants to Human and Bovine Serum Albumin

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Abstract
The interaction of acenocoumarin, coumachlor, phenprocoumon, and warfarin with human and bovine serum albumin was investigated by ultracentrifugation and circular dichroism measurements. Although all four drugs generate extrinsic Cotton effects when bound to human and bovine serum albumin, large differences in the signs and the intensities of the Cotton effects are observed. The differences in the induced Cotton effects suggest differential molecular binding mechanisms.