Premium
Spectroscopic study of the interaction between lycopene and bovine serum albumin
Author(s) -
Rodríguez Galdón Beatriz,
Pinto Corraliza Carmen,
Cestero Carrillo Juan J.,
Macías Laso Pedro
Publication year - 2012
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.2434
Subject(s) - circular dichroism , bovine serum albumin , lycopene , chemistry , quenching (fluorescence) , fluorescence , fluorescence spectroscopy , serum albumin , aqueous solution , chromatography , crystallography , biochemistry , carotenoid , organic chemistry , physics , quantum mechanics
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. Copyright © 2012 John Wiley & Sons, Ltd.