Spectroscopic analysis of the binding of amylobarbitone, secbutobarbitone, pentobarbitone, phenobarbitone and quinalbarbitone to human serum albumin.

The binding of five barbiturates: amylobarbitone, secbutobarbitone, pentobarbitone, phenobarbitone and quinalbarbitone to human serum albumin (HSA) was studied by difference spectroscopy and spectrofluorimetric titrations. There were no changes in the HSA spectral properties. Our result suggest that there are two classes of binding sites on HSA for these barbiturates. A detailed investigation of the effect of their binding to HSA by deconvoluted spectra, suggests that the interaction of barbiturate-HSA takes place principally on the subdomain IIIA of HSA.