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...
Hoofdauteurs: | , , , , , |
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Formaat: | Journal article |
Taal: | English |
Gepubliceerd in: |
2004
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_version_ | 1826297753866600448 |
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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. |
first_indexed | 2024-03-07T04:36:29Z |
format | Journal article |
id | oxford-uuid:d0183eb0-cd50-4263-923c-67d6d02d933c |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T04:36:29Z |
publishDate | 2004 |
record_format | dspace |
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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