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Spectroscopic study of the interaction between lycopene and bovine serum albumin.


Luminescence. 2012 Sep 25;


Authors: Rodríguez Galdón B, Pinto Corraliza C, Cestero Carrillo JJ, Macías Laso P


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. Copyright © 2012 John Wiley & Sons, Ltd.

PMID: 23008219 [PubMed - as supplied by publisher]