Spectroscopic Analysis of the Binding of Amylobarbitone, Secbutobarbitone, Pentobarbitone, Phenobarbitone and Quinalbarbitone to Human Serum Albumin

Author:

González-Jimènez J1,Moreno F1,Blanco F Garcìa1

Affiliation:

1. Instituto Pluridisciplinar, Departamento de Quimica Fisica Farmaceutica, Facultad de Farmacia, 28040 Madrid, Spain

Abstract

Abstract The binding of five barbiturates: amylobarbitone, secbutobarbitone, pentobarbitone, phenobarbitone and quinalbarbitone to human serum albumin (HSA) was studied by difference spectroscopy and spectro-fluorimetric 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.

Publisher

Oxford University Press (OUP)

Subject

Pharmaceutical Science,Pharmacology

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4. Binding of thiopental to human serum albumin in presence of halogenated hydrocarbons and ethers;Buch;Methods Find. Exp. Clin. Pharmacol.,1990

5. Relationship between the solubility parameter and the binding of drugs by plasma protein;Bustamante;J. Pharm. Sci.,1986

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