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Turning on Protein Function Inhibited by DNA Aptamers Employing a Covalent DNA-Binding Protein.

Takeru Kanazu1,2, Erika Komiya1,2, Daimei Miura1,3

  • 1Department of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-8588, Japan.

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Summary

Uracil-DNA glycosylase (UdgX) can rapidly reverse DNA aptamer inhibition, restoring protein function. This enzyme offers a versatile method for controlling aptamer activity in therapeutic applications.

Keywords:
AnticoagulantDNA aptamerDNA aptamer removerUdgXuracil-DNA glycosylase

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oligonucleotide Therapeutics

Background:

  • DNA aptamers are effective inhibitors but their action is unidirectional.
  • Releasing aptamers from target complexes can enhance their therapeutic utility.
  • Uracil-DNA glycosylase from Mycobacterium smegmatis (UdgX) covalently binds DNA post-uracil removal.

Purpose of the Study:

  • To investigate the use of UdgX for reversing DNA aptamer-mediated inhibition.
  • To assess UdgX's efficacy in restoring protein function inhibited by aptamers.

Main Methods:

  • Incorporated uracil-DNA into a G-quadruplex DNA aptamer targeting thrombin.
  • Introduced UdgX to cleave the uracil-containing DNA, releasing the aptamer.
  • Assessed restoration of thrombin activity and anti-VEGF antibody binding.

Main Results:

  • UdgX rapidly restored thrombin activity (nearly 100% in 1 min) exceeding complementary strand addition.
  • UdgX successfully restored bevacizumab binding inhibited by a hairpin aptamer.
  • Demonstrated UdgX's speed and efficacy in reversing aptamer inhibition.

Conclusions:

  • UdgX provides a fast and efficient method to reverse DNA aptamer inhibition.
  • UdgX shows versatile potential for reactivating protein functions targeted by aptamers.
  • This approach offers a promising strategy for controlling aptamer activity in therapeutics.