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Modulating G-quadruplex/hemin DNAzyme peroxidase-mimicking activity via mechanochemical coupling
Hui Zhang1, Shengjie Gao1, Zhiwen Guan1
1School of Food and Biological Engineering, Hefei University of Technology, Hefei, 230009, China.
Analytica Chimica Acta
|January 16, 2026
Summary
This study introduces a mechanochemical strategy using DNA clamps to boost G-quadruplex (G4)/hemin DNAzyme activity and stability. This approach enhances catalytic efficiency and robustness against environmental interference, advancing biosensing applications.
Area of Science:
- Biochemistry
- Nanotechnology
- Catalysis
Background:
- G-quadruplex (G4) DNAzyme, a hemin complex, mimics peroxidase activity.
- It offers advantages like low cost, biocompatibility, and ease of synthesis for biosensing and nanotechnology.
- Limitations include low catalytic activity and challenges in dynamic regulation.
Purpose of the Study:
- To develop a mechanochemical strategy for enhancing and modulating G4/Hemin DNAzyme activity.
- To improve the enzyme's robustness in complex environments, specifically against lead ion interference.
Main Methods:
- Utilized double-stranded DNA (dsDNA) as molecular clamps to mechanically interact with G4/Hemin.
- Employed mechanochemical force to perturb G4 conformation and modulate enzyme activity.
- Assessed G4/Hemin activity and resistance to Pb2+ interference under modulated conditions.
Main Results:
- A straightforward mechanochemical strategy using dsDNA molecular clamps successfully enhanced G4/Hemin DNAzyme activity.
- Activity enhancement was attributed to conformational changes induced by mechanical stretching, increasing Vmax or Kcat.
- The strategy significantly improved resistance to Pb2+ interference, maintaining high activity at 10 μM Pb2+.
Conclusions:
- The mechanochemical approach effectively addresses limitations of low activity and poor environmental robustness in G4/Hemin DNAzymes.
- This method provides a transformative tool for developing advanced biosensing and catalytic applications.
- The findings open new avenues for dynamic regulation and performance optimization of DNAzymes.
