Elucidating the binding mechanism between bovine serum albumin and TiO2 nanoparticles with diverse properties: Insights from spectroscopic methods and molecular docking simulation

The interaction mechanism between bovine serum albumin (BSA) and titanium dioxide (TiO2) nanoparticles with different shapes, surface charge and hydrophobic properties was studied using multiple spectral methods and molecular docking simulation. UV-vis spectra showed that when BSA interacted with the four TiO2 NPs, the TiO2 nanoparticles and BSA formed a stable ground state complex. Fluorescence spectra showed that the binding capacities of four different types of TiO2 nanoparticles with BSA are as follows: spherical TiO2 (s-TiO2) > rodshaped TiO2 (r-TiO2) > positively charged TiO2 (c-TiO2) > hydrophobic TiO2 (h-TiO2). The results of synchronous fluorescence, circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy revealed that sTiO2, r-TiO2, and c-TiO2 have a weak effect on the conformation of BSA, whereas h-TiO2 has a greater effect. Molecular docking and MD simulations results show that the content of hydroxyl groups plays a key role in the binding capacity.

Automated summary

The interaction mechanism between bovine serum albumin (BSA) and titanium dioxide (TiO2) nanoparticles of different shapes, surface charges, and hydrophobic properties was studied. The results showed that the binding capacities of the nanoparticles with BSA varied, with spherical TiO2 > rod-shaped TiO2 > positively charged TiO2 > hydrophobic TiO2. The conformation of BSA was minimally affected by spherical, rod-shaped, and positively charged TiO2, while hydrophobic TiO2 had a greater effect. Molecular docking and MD simulations indicated that the content of hydroxyl groups played a key role in the binding capacity.