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We have recently described the isolation of 2'-fluoropyrimidine-substituted RNA aptamers that bind selectively to disease-associated beta-sheet-rich forms of the prion protein, PrP, from a number of mammalian species. These aptamers inhibit the accumulation of protease-resistant forms of PrP in a prion-seeded, in vitro conversion assay. Here we identify the minimal portions of two of these aptamers that retain binding specificity. We determine their secondary structures by a combination of modeling and solution probing. Finally, we identify an internal site for biotinylation of a minimized, synthetic aptamer and use the resultant reagent in the detection of abnormal forms of PrP in vitro.

Original publication




Journal article


J Biol Chem

Publication Date





13102 - 13109


Animals, Base Sequence, Binding Sites, Biotinylation, Cattle, Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Kinetics, Molecular Sequence Data, Prions, Protein Binding, Protein Conformation, Protein Folding, Protein Structure, Secondary, RNA, Transcription, Genetic, Urea