Structural determinants of conformationally selective, prion-binding aptamers.

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...

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Bibliografische gegevens
Hoofdauteurs: Sayer, N, Cubin, M, Rhie, A, Bullock, M, Tahiri-Alaoui, A, James, W
Formaat: Journal article
Taal:English
Gepubliceerd in: 2004
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author Sayer, N
Cubin, M
Rhie, A
Bullock, M
Tahiri-Alaoui, A
James, W
author_facet Sayer, N
Cubin, M
Rhie, A
Bullock, M
Tahiri-Alaoui, A
James, W
author_sort Sayer, N
collection OXFORD
description 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.
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spelling oxford-uuid:d0183eb0-cd50-4263-923c-67d6d02d933c2022-03-27T07:47:35ZStructural determinants of conformationally selective, prion-binding aptamers.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d0183eb0-cd50-4263-923c-67d6d02d933cEnglishSymplectic Elements at Oxford2004Sayer, NCubin, MRhie, ABullock, MTahiri-Alaoui, AJames, WWe 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.
spellingShingle Sayer, N
Cubin, M
Rhie, A
Bullock, M
Tahiri-Alaoui, A
James, W
Structural determinants of conformationally selective, prion-binding aptamers.
title Structural determinants of conformationally selective, prion-binding aptamers.
title_full Structural determinants of conformationally selective, prion-binding aptamers.
title_fullStr Structural determinants of conformationally selective, prion-binding aptamers.
title_full_unstemmed Structural determinants of conformationally selective, prion-binding aptamers.
title_short Structural determinants of conformationally selective, prion-binding aptamers.
title_sort structural determinants of conformationally selective prion binding aptamers
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