Glutathione significantly inhibits the nanozymatic activity of N-doped carbon dots

Herein, the effect of the glutathione molecules (a possible inhibitor) on the peroxidase-like activity of the enzyme-like N-doped carbon dots was evaluated. To do this investigation, the enzyme-like activity of N-doped carbon dots was evaluated toward peroxidase-mediated oxidation of TMB as a common peroxidase substrate, revealing high intrinsic peroxidase-like activity of N-doped carbon dots. However, the intrinsic peroxidase-like activity of the N-doped carbon dot was significantly inhibited by the introduction of the glutathione molecules in the reaction media. Hence, the inhibitory effect of glutathione molecules on their nanozymatic activity was evaluated as a function of enzyme-like residual activity in the presence of glutathione molecules. The results reveal that the relative activity of nanozymes was inhibited by increasing the glutathione concentration in the reaction media and reached its minimum value (45%) when the glutathione concentration was 14 µM and then leveled off.