Investigations into the binding of phenprocoumon to albumin using fluorescence spectroscopy

Abstract

Abstract The fluorescence of phenprocoumon is enhanced following interaction with bovine and human serum albumin, allowing the binding parameters for two binding sites to be estimated by a modified Bjerrum method and the Scatchard method. The fluorescence is increased as the pH is raised to 9·0 and also on addition of the drugs ibuprofen and fenoprofen. Chloride ions, phenylbutazone and acenocoumarin seem to displace phenprocoumon from its primary binding site on human serum albumin. Investigations with the enantiomers of phenprocoumon show that the binding sites have some stereospecificity.