Journal
SENSORS AND ACTUATORS B-CHEMICAL
Volume 335, Issue -, Pages -Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.snb.2021.129671
Keywords
Nanozyme; ATP; Peroxidase; Laccase; H2O2
Funding
- National Natural Science Foundation of China [21705132]
- Fundamental Research Fund for the Central Universities [XDJK2019TY003]
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This study introduces a facile method for fabricating metal-ATP nanoparticles and demonstrates that the enzyme-like activities of these nanoparticles can be modulated by metal doping. The CuMnFe-ATP NPs exhibit multiple enzyme-like activities, showing potential applications in the field of biosensing.
This paper reports a facile approach for fabricating metal-adenosine triphosphate (ATP) nanoparticles (NPs) by the self-assembly of ATP and metal ions under moderate conditions. Here, Cu-ATP NPs only showed laccase-like activity, but the Fe3+-doped Cu-ATP NPs could exhibit peroxidase-like activity, resulting in a decrease in laccase-like activity. Mn2+ ions functioned as a regulator to balance the enzyme-like activities of CuFe-ATP NPs, endowing the CuMnFe-ATP NPs with both strong laccase- and peroxidase-like activities. Surprisingly, the CuMnFe-ATP NPs also exhibited catalase-like activity under neutral conditions, improving the efficiency of phenol oxidation. X-ray photoelectron spectroscopy (XPS) analysis confirmed that the mixed valence states of the metals in the CuMnFe-ATP NPs accounted for the high catalytic efficiency; also, the large surface area and intrinsic porosity of the NPs were of great importance. The kinetic studies results indicated that the CuMnFe-ATP NPs exhibited rather strong affinities to 3,3,5',5'-tetramethylbenzidine (TMB) and 2, 4-dichlorophenol (2,4-DP). On the basis of peroxidase-mimic activity, the CuMnFe-ATP NP system was employed to establish a facile colorimetric biosensing method for H2O2 determination, and the detection limit of H2O2 was 0.047 mu mol.L-1. These results prove that the enzyme-like activities of Cu-ATP NPs can be modulated via simple metal doping, which may extend to other nanozymes.
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