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Microchimica Acta

, 186:514 | Cite as

In-situ generation of nanozymes by natural nucleotides: a biocatalytic label for quantitative determination of hydrogen peroxide and glucose

  • Guiqian Wang
  • Lisha Feng
  • Wei Li
  • Jinli Zhang
  • Yan FuEmail author
Original Paper
  • 70 Downloads

Abstract

Four natural nucleotides including 5′-cytidine monophosphate (CMP), 5′-thymidine monophosphate (TMP), guanosine monophosphate (GMP) and 5′-adenosine monophosphate (AMP) were employed to modulate the coordination environment and the valence state of PtCl42−. This is the first report that natural nucleotides have the ability to produce highly active Pt nanoclusters. The latter are shown to act as peroxidase mimetics. Both the size distribution and the charge state of Pt-nucleotide nanozymes vary with the chemical structures of nucleotides, thereby contributing to distinct enzyme-like activities. By adopting Pt-CMP as a signal amplifier, a photometric assay was well-established for quantitative determination of glucose. The assay is based on the oxidation of glucose by glucose oxidase. The oxidation product (H2O2) is detected at 652 nm via the Pt-CMP-catalyzed oxidation of 3,3′,5,5′-tetramethylbenzidine with H2O2. Response is linear in the 5 to 100 μM glucose concentration range, and the limit of detection is 0.12 μM (at S/N= 3). The method excels by a low signal background, high sensitivity, and low consumption of energy and materials.

Graphical abstract

Peroxidase mimicking Pt nanoclusters were synthesized by employing natural nucleotides as both the reducing agent and the stabilization template.

Keywords

Platinum Peroxidase Nanocluster Detection Nanocatalyst 

Notes

Acknowledgements

This study was funded by National Natural Science Foundation of China (21878225, 21776215).

Compliance with ethical standards

The author(s) declare that they have no competing interests.

Supplementary material

604_2019_3616_MOESM1_ESM.docx (2.6 mb)
ESM 1 (DOCX 2.63 mb)

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Copyright information

© Springer-Verlag GmbH Austria, part of Springer Nature 2019

Authors and Affiliations

  1. 1.School of Chemical Engineering and TechnologyTianjin UniversityTianjinPeople’s Republic of China
  2. 2.School of Chemistry and Chemical EngineeringYunnan Open UniversityKunmingPeople’s Republic of China

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