Effects of TiO2 nanoparticles on the kinetics and conformation of bovine alkaline phosphatase.

This study observed the interaction between titanium dioxide (TiO2) nanoparticles and bovine intestinal alkaline phosphatase (BALP) through a combination of spectroscopic techniques and enzymatic activity assays. Fluorescence spectroscopy suggested that a static quenching mechanism governs the interaction, supported by the binding constant and site number determined at three temperatures. The predominant forces involved in the nanoparticle-protein complex were identified as hydrogen bonding and van der Waals interactions. Circular dichroism analysis indicated substantial alterations in both secondary and tertiary structures of BALP in the presence of TiO2. Moreover, enzymatic assays revealed that TiO2 acts as an uncompetitive inhibitor, reducing the enzyme's activity. These findings provide valuable insight into the conformational and functional consequences of TiO2 nanoparticle interaction with proteins.