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Related Experiment Videos

Structural determinants of conformationally selective, prion-binding aptamers.

Natalie M Sayer1, Matthew Cubin, Alexandre Rhie

  • 1Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, United Kingdom.

The Journal of Biological Chemistry
|January 9, 2004
PubMed
Summary

Researchers developed novel RNA aptamers targeting disease-associated prion protein (PrP). These aptamers inhibit PrP accumulation and can detect abnormal PrP forms in vitro, offering potential diagnostic tools.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Prion diseases are associated with abnormal beta-sheet-rich forms of the prion protein (PrP).
  • RNA aptamers have emerged as potential therapeutic and diagnostic agents.
  • Selective targeting of disease-associated PrP forms is crucial for understanding and treating prion diseases.

Purpose of the Study:

  • To identify minimal RNA aptamer sequences with retained binding specificity for disease-associated prion protein (PrP).
  • To determine the secondary structures of these minimized aptamers.
  • To develop a biotinylated aptamer reagent for detecting abnormal PrP forms.

Main Methods:

  • Isolation and characterization of 2'-fluoropyrimidine-substituted RNA aptamers.
  • In vitro prion-seeded conversion assays to assess aptamer inhibition of PrP accumulation.

Related Experiment Videos

  • Secondary structure determination using computational modeling and solution probing.
  • Biotinylation of a minimized aptamer for detection assays.

    • Main Results:

    • Identified minimal aptamer portions retaining selective binding to disease-associated PrP.
    • Determined the secondary structures of these functional aptamer fragments.
    • Successfully created a biotinylated aptamer reagent for in vitro detection of abnormal PrP.

    Conclusions:

    • Minimized RNA aptamers retain specific binding to disease-associated PrP.
    • These aptamers can inhibit PrP accumulation and are useful for detecting abnormal PrP.
    • The developed biotinylated aptamer is a promising tool for prion disease diagnostics.