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Related Concept Videos

Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis
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Generating Biologically Stable TNA Aptamers that Function with High Affinity and Thermal Stability.

Matthew R Dunn, Cailen M McCloskey, Patricia Buckley1

  • 1U.S. Army CCDC Chemical Biological Center, APG, Maryland 21010, United States.

Journal of the American Chemical Society
|April 17, 2020
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This study introduces a novel xeno-nucleic acid, α-l-threofuranosyl nucleic acid (TNA), which is resistant to nuclease digestion. TNA aptamers targeting HIV reverse transcriptase show high affinity and stability, offering potential for new diagnostic and therapeutic tools.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Nucleic Acid Chemistry

Background:

  • Aptamers are limited in biomedical applications due to susceptibility to nuclease degradation.
  • Xeno-nucleic acids offer potential for enhanced stability and functionality.

Purpose of the Study:

  • To develop a nuclease-resistant aptamer system using α-l-threofuranosyl nucleic acid (TNA).
  • To isolate and characterize TNA aptamers with high binding affinity for HIV reverse transcriptase (HIV RT).

Main Methods:

  • Development of an engineered TNA polymerase for aptamer synthesis.
  • Isolation of TNA aptamers targeting HIV RT using a display strategy.
  • Characterization of binding affinity (KD) and thermal stability.

Main Results:

  • TNA aptamers demonstrated complete resistance to nuclease digestion.
  • Isolated TNA aptamers bound HIV RT with high affinity (KDs of 0.4-4.0 nM).
  • TNA aptamers exhibited superior thermal stability compared to monoclonal antibodies.

Conclusions:

  • TNA aptamers represent a biologically stable and highly affine alternative to traditional aptamers.
  • The nuclease resistance and thermal stability of TNA aptamers are advantageous for diagnostic and therapeutic applications.
  • This TNA system provides a powerful platform for developing novel biomedical agents.