Binding Mechanism of Bovine Serum Albumin to Troxerutin by Synchronous Fluorescence Spectroscopy and Chemometrics

Previous works have reported the binding of Bovine Serum Albumin (BSA) to troxerutin by absorption and fluorescence spectroscopy. In order to extend the investigation of their binding characteristics, the study presented here was designed to evaluate their interaction by the synchronous fluorescence spectroscopy and Multivariate Curve Resolution With Alternating Least Squares (MCR-ALS) under simulative physiological conditions. The Evolving Factor Analysis (EFA) and MCR-ALS analysis results show that there are three chemical species in the troxerutin-BSA system, which reveal that the fluorescence quenching of BSA caused by troxerutin may be a static quenching mechanism. The spectral profile of each compound was obtained by the soft of MCR-ALS. The obtained average binding constant is 6.43×10⁵ mol^-1 L for BSA and troxerutin concentration ratio is 7 while that is 6.89×10⁵ mol^-1 L for troxerutin and BSA concentration ratio is 5. The study might further help us to better understand the structural features and toxicological action of troxerutin at the molecular level.