A spectroscopy approach for the study of the interactions of bioactive vanadium species with bovine serum albumin

The interest in biological functions (benefits or toxics effects) of vanadium species has grown enormously in recent years. In this work, different spectroscopic methods were applied to study the effects of the interaction of vanadyl and vanadate species with bovine serum albumin (BSA), considered as the most abundant plasma protein. UV–Vis, Fourier transform infrared (FT-IR), and FT-Raman spectroscopies were used to investigate changes in secondary and tertiary structures of BSA induced by the binding of oxovanadium(IV) and vanadate(V) species (VO2+ and VO3-, respectively). Correlations between the metal ion binding mode, protein conformational transitions, and structural variations were established.

In this article, Fourier transform infrared spectroscopy (FT-IR) and Raman spectroscopy were used to investigate the changes in BSA structure, particularly in its secondary and tertiary structures in the presence of bioactive vanadium species.Figure optionsDownload as PowerPoint slide