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In Vitro Selection of an ATP-Binding TNA Aptamer

Recent advances in polymerase engineering have made it possible to isolate aptamers from libraries of synthetic genetic polymers (XNAs) with backbone structures that are distinct from those found in nature. However, nearly all of the XNA aptamers produced thus far have been generated against protein...

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Detalles Bibliográficos
Autores principales: Zhang, Li, Chaput, John C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7570665/
https://www.ncbi.nlm.nih.gov/pubmed/32933142
http://dx.doi.org/10.3390/molecules25184194
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author Zhang, Li
Chaput, John C.
author_facet Zhang, Li
Chaput, John C.
author_sort Zhang, Li
collection PubMed
description Recent advances in polymerase engineering have made it possible to isolate aptamers from libraries of synthetic genetic polymers (XNAs) with backbone structures that are distinct from those found in nature. However, nearly all of the XNA aptamers produced thus far have been generated against protein targets, raising significant questions about the ability of XNA aptamers to recognize small molecule targets. Here, we report the evolution of an ATP-binding aptamer composed entirely of α-L-threose nucleic acid (TNA). A chemically synthesized version of the best aptamer sequence shows high affinity to ATP and strong specificity against other naturally occurring ribonucleotide triphosphates. Unlike its DNA and RNA counterparts that are susceptible to nuclease digestion, the ATP-binding TNA aptamer exhibits high biological stability against hydrolytic enzymes that rapidly degrade DNA and RNA. Based on these findings, we suggest that TNA aptamers could find widespread use as molecular recognition elements in diagnostic and therapeutic applications that require high biological stability.
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spelling pubmed-75706652020-10-28 In Vitro Selection of an ATP-Binding TNA Aptamer Zhang, Li Chaput, John C. Molecules Article Recent advances in polymerase engineering have made it possible to isolate aptamers from libraries of synthetic genetic polymers (XNAs) with backbone structures that are distinct from those found in nature. However, nearly all of the XNA aptamers produced thus far have been generated against protein targets, raising significant questions about the ability of XNA aptamers to recognize small molecule targets. Here, we report the evolution of an ATP-binding aptamer composed entirely of α-L-threose nucleic acid (TNA). A chemically synthesized version of the best aptamer sequence shows high affinity to ATP and strong specificity against other naturally occurring ribonucleotide triphosphates. Unlike its DNA and RNA counterparts that are susceptible to nuclease digestion, the ATP-binding TNA aptamer exhibits high biological stability against hydrolytic enzymes that rapidly degrade DNA and RNA. Based on these findings, we suggest that TNA aptamers could find widespread use as molecular recognition elements in diagnostic and therapeutic applications that require high biological stability. MDPI 2020-09-13 /pmc/articles/PMC7570665/ /pubmed/32933142 http://dx.doi.org/10.3390/molecules25184194 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Zhang, Li
Chaput, John C.
In Vitro Selection of an ATP-Binding TNA Aptamer
title In Vitro Selection of an ATP-Binding TNA Aptamer
title_full In Vitro Selection of an ATP-Binding TNA Aptamer
title_fullStr In Vitro Selection of an ATP-Binding TNA Aptamer
title_full_unstemmed In Vitro Selection of an ATP-Binding TNA Aptamer
title_short In Vitro Selection of an ATP-Binding TNA Aptamer
title_sort in vitro selection of an atp-binding tna aptamer
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7570665/
https://www.ncbi.nlm.nih.gov/pubmed/32933142
http://dx.doi.org/10.3390/molecules25184194
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