title: Spectroscopic study of the interaction between lycopene and bovine serum albumin.
abstract: The interaction of lycopene with bovine serum albumin (BSA) in aqueous solution was studied by fluorescence quenching, three-dimensional fluorescence and circular dichroism spectroscopy. The data showed that the fluorescence of BSA was quenched by lycopene at different temperatures through a dynamic mechanism. The evaluation of three-dimensional fluorescence spectra revealed a conformational modification of BSA induced by coupling with lycopene and an increase in protein diameter as a consequence of the ligand-protein interaction. Moreover, the information obtained from evaluation of the effect of lycopene on BSA conformation by circular dichroism strongly supported the existence of a slight unfolding of BSA induced by coupling to lycopene.
authors.affiliation: Department of Biochemistry and Molecular Biology, Faculty of Sciences, Extremadura University, Av. Elvas s/n, 06006, Badajoz, Spain.
authors.forename: Beatriz
authors.initials: B
authors.lastname: Rodríguez Galdón
authors.forename: Carmen
authors.initials: C
authors.lastname: Pinto Corraliza
authors.forename: Juan J
authors.initials: JJ
authors.lastname: Cestero Carrillo
authors.forename: Pedro
authors.initials: P
authors.lastname: Macías Laso
mesh_terms: D000818:Animals; D002338:Carotenoids / Q000737:chemistry*; D002417:Cattle; D002942:Circular Dichroism; D005453:Fluorescence; D000077276:Lycopene; D015394:Molecular Structure; D058767:Protein Unfolding; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
chemical_list: D012710:Serum Albumin, Bovine; D002338:Carotenoids; D000077276:Lycopene