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Selection of Aptamers for Amyloid &#946;-Protein, the Causative Agent of Alzheimer's Disease
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Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

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Aptamers Selected for Recognizing Amyloid β-Protein-A Case for Cautious Optimism.

Farid Rahimi1

  • 1Division of Biomedical Science and Biochemistry, Research School of Biology, The Australian National University, Canberra, ACT 2601, Australia. farid.rahimi@anu.edu.au.

International Journal of Molecular Sciences
|March 3, 2018
PubMed
Summary

Aptamers, or oligonucleotide ligands, face challenges in recognizing amyloid beta-protein (Aβ) due to Aβ's complex nature. Studies highlight the need for pure targets and specific aptamer characterization for successful Aβ recognition.

Keywords:
Alzheimer diseaseamyloid β-proteinantibodiescross-reactionsnucleotide aptamersoligonucleotide ligandsspecificitysystematic evolution of ligands by exponential enrichmenttherapeutics

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Aptamers are oligonucleotide ligands with broad molecular recognition capabilities.
  • Amyloid β-protein (Aβ) is intrinsically disordered, existing in dynamic, metastable states.
  • Aβ's role in Alzheimer disease pathogenesis is significant but debated.

Purpose of the Study:

  • To review aptamer applications for amyloid β-protein (Aβ) recognition.
  • To identify challenges and limitations in Aβ-aptamer studies.
  • To emphasize requirements for successful aptamer selection against Aβ.

Main Methods:

  • Literature review of aptamer selection studies targeting Aβ assemblies.
  • Analysis of reported interactions between aptamers and Aβ.
  • Evaluation of factors affecting aptamer specificity and efficacy.

Main Results:

  • Aptamer application to Aβ has been limited by Aβ's metastable nature and dynamic conformational ensembles.
  • Nonspecific interactions between aptamers and Aβ assemblies are frequently reported.
  • The inherent affinity of RNA oligonucleotides for β-sheet structures complicates Aβ recognition.

Conclusions:

  • Purity and uniformity of the Aβ target are crucial for reliable aptamer selection.
  • Rigorous characterization of aptamer specificity is essential for Aβ-targeting aptamers.
  • Overcoming challenges requires careful consideration of Aβ's properties and aptamer-target interactions.