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In vitro selection of RNA aptamers against a composite small molecule-protein surface
A particularly challenging problem in chemical biology entails developing systems for modulating the activity of RNA using small molecules. One promising new approach towards this problem exploits the phenomenon of ‘surface borrowing,’ in which the small molecule is presented to the RNA in complex w...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2005
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1240114/ https://www.ncbi.nlm.nih.gov/pubmed/16199752 http://dx.doi.org/10.1093/nar/gki867 |
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author | Plummer, Kelly A. Carothers, James M. Yoshimura, Masahiro Szostak, Jack W. Verdine, Gregory L. |
author_facet | Plummer, Kelly A. Carothers, James M. Yoshimura, Masahiro Szostak, Jack W. Verdine, Gregory L. |
author_sort | Plummer, Kelly A. |
collection | PubMed |
description | A particularly challenging problem in chemical biology entails developing systems for modulating the activity of RNA using small molecules. One promising new approach towards this problem exploits the phenomenon of ‘surface borrowing,’ in which the small molecule is presented to the RNA in complex with a protein, thereby expanding the overall surface area available for interaction with RNA. To extend the utility of surface borrowing to include potential applications in synthetic biology, we set out to create an ‘orthogonal’ RNA-targeting system, one in which all components are foreign to the cell. Here we report the identification of small RNA modules selected in vitro to bind a surface-engineered protein, but only when the two macromolecules are bound to a synthetic bifunctional small molecule. |
format | Text |
id | pubmed-1240114 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-12401142005-10-05 In vitro selection of RNA aptamers against a composite small molecule-protein surface Plummer, Kelly A. Carothers, James M. Yoshimura, Masahiro Szostak, Jack W. Verdine, Gregory L. Nucleic Acids Res Article A particularly challenging problem in chemical biology entails developing systems for modulating the activity of RNA using small molecules. One promising new approach towards this problem exploits the phenomenon of ‘surface borrowing,’ in which the small molecule is presented to the RNA in complex with a protein, thereby expanding the overall surface area available for interaction with RNA. To extend the utility of surface borrowing to include potential applications in synthetic biology, we set out to create an ‘orthogonal’ RNA-targeting system, one in which all components are foreign to the cell. Here we report the identification of small RNA modules selected in vitro to bind a surface-engineered protein, but only when the two macromolecules are bound to a synthetic bifunctional small molecule. Oxford University Press 2005 2005-09-30 /pmc/articles/PMC1240114/ /pubmed/16199752 http://dx.doi.org/10.1093/nar/gki867 Text en © The Author 2005. Published by Oxford University Press. All rights reserved |
spellingShingle | Article Plummer, Kelly A. Carothers, James M. Yoshimura, Masahiro Szostak, Jack W. Verdine, Gregory L. In vitro selection of RNA aptamers against a composite small molecule-protein surface |
title | In vitro selection of RNA aptamers against a composite small molecule-protein surface |
title_full | In vitro selection of RNA aptamers against a composite small molecule-protein surface |
title_fullStr | In vitro selection of RNA aptamers against a composite small molecule-protein surface |
title_full_unstemmed | In vitro selection of RNA aptamers against a composite small molecule-protein surface |
title_short | In vitro selection of RNA aptamers against a composite small molecule-protein surface |
title_sort | in vitro selection of rna aptamers against a composite small molecule-protein surface |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1240114/ https://www.ncbi.nlm.nih.gov/pubmed/16199752 http://dx.doi.org/10.1093/nar/gki867 |
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