Titanium dioxide nanoparticles (TiO2 NP) are widely used across various industries due to their unique properties. However, their potential to penetrate biological systems and cause adverse effects necessitates a comprehensive understanding of their interactions with biological molecules. This study investigates the interaction between mitochondrial aspartate aminotransferase (mAspAT) and TiO2 NP, uncoated and coated with dextran sulphate, to evaluate their impact on the enzyme's catalytic properties.TiO2 NP was synthesised, suspended in deionized water, and subjected to ultrasound treatment. The enzyme activity of mAspAT was measured in mixtures containing both the supernatant and the precipitate with adsorbed nanoparticles. The interaction of TiO2 NP with mAspAT was assessed by measuring the enzyme activity distribution between the supernatant and precipitate fractions. Most enzymes did not bind to uncoated nanoparticles and remained in the supernatant after suspension. The findings showed that dextran sulphate-coated nanoparticles made mAspAT bind more strongly, which greatly decreased the enzyme's activity. This underscores the crucial role of surface modifications in modulating enzyme interactions and activity, providing valuable insights for designing nanomaterials in biomedical applications
Key words: uncoated, coated titanium dioxide nanoparticles, mitochondrial aspartate aminotransferase, enzyme interaction, nanomaterials
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