Unraveling Prion Protein Interactions with Aptamers and Other PrP-Binding Nucleic Acids

International Journal of Molecular Sciences
Bruno Macedo, Yraima Cordeiro

Abstract

Transmissible spongiform encephalopathies (TSEs) are a group of neurodegenerative disorders that affect humans and other mammals. The etiologic agents common to these diseases are misfolded conformations of the prion protein (PrP). The molecular mechanisms that trigger the structural conversion of the normal cellular PrP (PrPC) into the pathogenic conformer (PrPSc) are still poorly understood. It is proposed that a molecular cofactor would act as a catalyst, lowering the activation energy of the conversion process, therefore favoring the transition of PrPCto PrPSc. Several in vitro studies have described physical interactions between PrP and different classes of molecules, which might play a role in either PrP physiology or pathology. Among these molecules, nucleic acids (NAs) are highlighted as potential PrP molecular partners. In this context, the SELEX (Systematic Evolution of Ligands by Exponential Enrichment) methodology has proven extremely valuable to investigate PrP-NA interactions, due to its ability to select small nucleic acids, also termed aptamers, that bind PrP with high affinity and specificity. Aptamers are single-stranded DNA or RNA oligonucleotides that can be folded into a wide range of structures (from harpi...Continue Reading

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Citations

Nov 17, 2017·International Journal of Molecular Sciences·Pascal RöthlisbergerMarcel Hollenstein
Mar 3, 2018·International Journal of Molecular Sciences·Farid Rahimi
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Aug 11, 2020·Nucleic Acids Research·Eric Vallabh MinikelSonia M Vallabh
Nov 23, 2021·Journal of Molecular Biology·Aishwarya Agarwal, Samrat Mukhopadhyay

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Methods Mentioned

BETA
SELEX
light scattering
nuclear
X-ray
PCR
in vitro transcription
electrophoresis
chemical modification
NMR
electron microscopy

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