Conformational and functional changes of bovine serum albumin induced by TiO2 nanoparticles binding

Abstract In the present study, we have investigated the thermal stability of bovine serum albumin (BSA) in the presence of TiO 2 nanoparticles (TiO 2 NPs). The effects of TiO 2 NPs on the transportation function of BSA were also studied by fluorescence spectral method. The circular dichroism (CD) study revealed that addition of TiO 2 NPs moderately decreased the α-Helix content of the protein with the abruptly changing its tertiary structure by hydrogen bonding, van der Waals or electrostatic forces. It has been found that TiO 2 NPs acted as a structure destabilizer for BSA during the thermal denaturation process. The fluorescence quenching and molecular modeling data indicated the existence of strong interaction between BSA and the TiO 2 NPs surface that changed the binding affinities of some ligands for BSA, implying that TiO 2 NPs in blood will affect the transporting ability of serum albumin.