Spectroscopic studies on the toxic interaction of sodium oleate with bovine serum albumin.

The effects of sodium oleate on Bovine Serum Albumin (BSA) were investigated by fluorescence, synchronous fluorescence, ultraviolet-visible and circular dichroism spectroscopy. According to the experiment results, we found that the fluorescence intensity of BSA was quenched by sodium oleate following a static mode, a sodium oleate-BSA complex was formed and the binding site was calculated approximately equal to 1. The experimental results showed that the hydrophilic group (-COONa) can bind to the BSA and lead to the looser of the protein conformation, the microenvironment and the secondary structure elements were changed in the presence of sodium oleate. This work reflected the toxic interaction mechanism of BSA and sodium oleate from the perspective of spectroscopy. © Springer Science+Business Media, LLC 2010