title: Interaction of emodin, aloe-emodin, and rhein with human serum albumin: a fluorescence spectroscopic study.
abstract: The interaction of the dihydroxyanthraquinones, emodin (1), aloe-emodin (2), and rhein (3) with human serum albumin (HSA) has been studied through fluorescence spectroscopy. Quenching studies and the association constant of the anthraquinoid compounds 1, 2, and 3 in the presence of HSA were estimated. The binding and quenching studies suggest that only emodin (1) may serve as a useful fluorescence probe for structure/function studies of different emodin binding proteins. No photoinduced binding was observed after irradiation of compounds 1, 2, and 3 in presence of human serum albumin.
authors.affiliation: Laboratorio de Fotoquímica, Centro de Química, Instituto Venezolano de Investigaciones Científicas I.V.I.C., Caracas, Venezuela.
authors.forename: F
authors.initials: F
authors.lastname: Vargas
authors.forename: C
authors.initials: C
authors.lastname: Rivas
authors.forename: M
authors.initials: M
authors.lastname: Medrano