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Studies of the Activity of Peroxidase-Like DNAzyme by Modifying 3′- or 5′-End of Aptamers

  1. Ming Zhang1,3,
  2. Haiqun Li1,
  3. Minggang Deng1,
  4. Xiaocheng Weng1,*,
  5. Heng Ma1,
  6. Shuo Feng1,
  7. Yangyang Zhou1,
  8. Xiang Zhou1,2,*

Article first published online: 17 JAN 2012

DOI: 10.1002/cbdv.201100040

Issue

Chemistry & Biodiversity

Chemistry & Biodiversity

Volume 9, Issue 1, pages 170–180, January 2012

Additional Information

How to Cite

Zhang, M., Li, H., Deng, M., Weng, X., Ma, H., Feng, S., Zhou, Y. and Zhou, X. (2012), Studies of the Activity of Peroxidase-Like DNAzyme by Modifying 3′- or 5′-End of Aptamers. Chemistry & Biodiversity, 9: 170–180. doi: 10.1002/cbdv.201100040

Author Information

  1. 1

    College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, P. R. of China (phone: +86-27-61056559; fax: +86-27-87336380)

  2. 2

    Key Laboratory of Biomedical Polymers of Ministry of Education, State Key Laboratory of Virology, Wuhan 430072, P. R. China

  3. 3

    College of Biological Environmental Sciences, Zhejiang Wali College, Ningbo, Zhejiang 315100, China

*College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, P. R. of China (phone: +86-27-61056559; fax: +86-27-87336380)

Publication History

  1. Issue published online: 17 JAN 2012
  2. Article first published online: 17 JAN 2012
  3. Manuscript Received: 3 FEB 2011

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Keywords:

  • DNAzymes;
  • Peroxidase;
  • Aptamers;
  • Hemin;
  • Structure[BOND]activity relationship (SAR)

Abstract

In the presence of hemin and under appropriate conditions, some modalities of G-quadruplexes can form a peroxidase-like DNAzyme that has been widely used in biology. Structure[BOND]function studies on the DNAzyme revealed that its catalytic ability may be dependent on the unimolecular parallel G-quadruplex. In this report, we present the preliminary investigation on the relationship between the structure and function of DNAzymes through a terminal oligo modification in G-quadruplex sequences by adding different lengths of oligo-dT to the 3′- or 5′-end of the aptamers. The results suggested that adding dTn to the 5′-end of the DNA sequence of the enzyme improved the ability of hemin to bind with DNA, but the addition of dTn to the 3′-end decreased the binding ability of hemin for DNA. The increased stability of the assembled DNAzyme would lead to more favorable binding between the enzyme and substrate (H2O2), facilitating higher peroxidase activity; on the contrary, with lower stability of the DNAzyme complex, we observed reduced peroxidase activity.

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