Study of the interaction between green Si quantum dots and bovine serum albumin via spectroscopic methods and its effects on antioxidant capacity and esterase activity.

Abstract

In this study, the interaction mechanism between Si quantum dots (SiQDs) and bovine serum albumin (BSA), as well as the conformational and functional alterations of BSA, were rigorously investigated via multispectral techniques and dynamic light scattering analysis. van der Waals forces and hydrogen bonding, as well as an exothermic reaction and a decrease in entropy, were the primary forces involved in the binding of SiQDs to BSA. In the binding process, SiQDs exhibit preferential proximity to Site I over other potential binding sites. Furthermore, the incorporation of SiQDs into BSA causes a reduction in the α-helix and β-sheet contents of the protein. This, in turn, leads to an increased degree of stretching and an increase in the hydrophilicity of BSA. Furthermore, the increase in the antioxidant capacity and esterase activity of BSA upon the addition of SiQDs was positively correlated with the concentration. These findings elucidate the underlying interaction mechanism between green fluorescence-emitting SiQDs and BSA and provide fundamental insights into both the biological and toxicological implications of SiQDs.