The binding of aryl carboxylic acid derivatives to human serum albumin--a structure-activity study.
The binding interactions of some aryl carboxylic acid derivatives have been examined by circular dichroism and fluorescence spectroscopy. With specific probes, we have shown that the seven ligands under study bind primarily to the benzodiazepine site on HSA. Their association constants are in the range of 10(5)-10(6) M-1 as found by spectropolarimetric titration, and appear to be closely related to some chemical features. It is concluded that the binding is enhanced by the lengthening of the carbon chain substituent with a terminating carboxyl moiety and by halogen substitution in the aromatic rings. It is further shown that hydrophilic substitutions such as hydroxyl or ketone groups in the carbon chain substituent will decrease the binding.
D001665:Binding Sites; D002264:Carboxylic Acids / Q000097:blood*; D002942:Circular Dichroism; D006801:Humans; D011048:Polarography; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013057:Spectrum Analysis / Q000379:methods; D013329:Structure-Activity Relationship
D002264:Carboxylic Acids; D012709:Serum Albumin