Captopril Molecules Reveal Strong pH-, Temperature-, And Concentration-Dependent Inhibitory Effect on Nanozymatic Activity of Peroxidase-Like Nitrogen-Doped Carbon Dots

Abstract

Saeed Reza Hormozi Jangi and Zahra Dehghani

Herein, peroxidase-like nitrogen-doped carbon dots were synthesized via a simple hydrothermal method and then characterized for their FL properties and enzyme-like activity. Thereafter, the effect of captopril molecules on their nanozymatic activity was evaluated by calculating their nanozymatic activity in the presence and absence of captopril, revealing a strong inhibitory effect of captopril on the nanozymatic behavior of peroxidase-like nitrogen-doped carbon dots. The effect of pH on the inhibitory effect of captopril (2 mg L-1) was evaluated over pH=2.0-6.0, revealing maximal and minimal inhibitory effect at pH=3.5 and pH=6.0, in order. The temperature-dependent inhibitory experiments exhibited a maximal inhibition percentage over 35-40 °C and a minimum inhibition percentage at 25 °C. Finally, the concentration-dependent inhibition was also checked in the presence of 0.0-8.0 mg L-1 of captopril, the results reveal that the relative activity of nanozymes was inhibited by increasing the inhibitor concentration and finally reached about 23% of its initial activity (i.e., 77% inhibition, inhibitor conc. of 8.0 mg L-1).

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