Interaction between titanium dioxide nanoparticles and human serum albumin revealed by fluorescence spectroscopy in the absence of photoactivation

Titanium dioxide (TiO2) nanoparticles (NPs) are widely used as an important kind of biomaterials. The interaction between TiO2 (P25) at 20 nm in diameter and human serum albumin (HSA) was studied by fluorescence spectroscopy in this work. Under the simulative physiological conditions, fluorescence data revealed the presence of a single class of binding site on HSA and its binding constants (Ka) were 2.18±0.04×104, 0.87±0.05×104, 0.68±0.06×104 M−1 at 298, 304 and 310 K, respectively. In addition, according to the Van't Hoff equation, the thermodynamic functions standard enthalpy (ΔH0) and standard entropy (ΔS0) for the reaction were calculated to be −75.18±0.15 kJ mol−1 and −170.11±0.38 J mol−1 K−1. These results indicated that TiO2 NPs bond to HSA mainly by van der Waals force and hydrogen bonding formation in low dielectric media, and the electrostatic interactions cannot be excluded. Furthermore, the effects of common ions on the binding constant of TiO2 NPs-HSA complex were discussed.