Adenine phosphate-Cu nanozyme with multienzyme mimicking activity for efficient degrading phenolic compounds and detection of hydrogen peroxide, epinephrine and glutathione

Abstract

BackgroundWith the development of nanotechnology, various nanomaterials with enzyme-like activity (nanozymes) have been reported. Due to their superior properties, nanozymes have shown important application potential in the fields of bioanalysis, disease detection, and environmental remediation. However, only a few nanomaterials with multi-enzyme mimicry activity have been reported. In this study, a novel multienzyme mimic was synthesized through a simple and rapid preparation protocol by coordinating copper ions with N3, N6 (amino), N7, and N9 on adenine phosphate. ResultsThe prepared adenine phosphate-Cu complex exhibits significant peroxidase, laccase, and oxidase mimicking activities. The Michaelis-Menten constant (Km) and the maximal velocity (Vmax) values of the peroxidase, laccase, and oxidase mimicking activities of AP-Cu nanozyme are 0.052 mM, 0.14 mM, and 2.49 mM; and 0.552 μM min−1, 6.70 μM min−1, and 2.24 μM min−1, respectively. Then, based on its laccase mimicking activity, the nanozyme was applied in the degradation of phenolic compounds. The calculated kinetic constant for the degradation of 2,4-dichlorophenol is 0.468 min−1 and the degradation efficiency of 2,4-dichlorophenol (0.1 mM) reaches 96.14% at 7 min. Finally, based on the multienzyme mimicking activity of adenine phosphate-Cu nanozyme, simple colorimetric sensing methods with high sensitivity and good selectivity were developed for the detection of hydrogen peroxide, epinephrine, and glutathione in the ranges of 20.0–200.0 μM (R2 = 0.9951), 5.0–100.0 μM (R2 = 0.9970), and 5.0–200.0 μM (R2 = 0.9924) with the limits of quantitation of 20.0 μM, 5.0 μM, and 5.0 μM, respectively. SignificanceIn short, the synthesis of nanozymes with multi-enzyme mimicry activity through coordination between copper ions and small molecule mimicry enzymes provides new ideas for the design and research of multi-enzyme mimics.