Investigating the properties of TBA variants with twin thrombin binding domains

In this paper, we report studies concerning thrombin binding aptamer (TBA) dimeric derivatives in which the 3′-ends of two TBA sequences have been joined by means of linkers containing adenosine or thymidine residues and/or a glycerol moiety. CD and electrophoretic investigations indicate that all m...

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Autores principales: Amato, Teresa, Virgilio, Antonella, Pirone, Luciano, Vellecco, Valentina, Bucci, Mariarosaria, Pedone, Emilia, Esposito, Veronica, Galeone, Aldo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6591170/
https://www.ncbi.nlm.nih.gov/pubmed/31235717
http://dx.doi.org/10.1038/s41598-019-45526-z
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author Amato, Teresa
Virgilio, Antonella
Pirone, Luciano
Vellecco, Valentina
Bucci, Mariarosaria
Pedone, Emilia
Esposito, Veronica
Galeone, Aldo
author_facet Amato, Teresa
Virgilio, Antonella
Pirone, Luciano
Vellecco, Valentina
Bucci, Mariarosaria
Pedone, Emilia
Esposito, Veronica
Galeone, Aldo
author_sort Amato, Teresa
collection PubMed
description In this paper, we report studies concerning thrombin binding aptamer (TBA) dimeric derivatives in which the 3′-ends of two TBA sequences have been joined by means of linkers containing adenosine or thymidine residues and/or a glycerol moiety. CD and electrophoretic investigations indicate that all modified aptamers are able to form G-quadruplex domains resembling that of the parent TBA structure. However, isothermal titration calorimetry measurements of the aptamer/thrombin interaction point to different affinities to the target protein, depending on the type of linker. Consistently, the best ligands for thrombin show anticoagulant activities higher than TBA. Interestingly, two dimeric aptamers with the most promising properties also show far higher resistances in biological environment than TBA.
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spelling pubmed-65911702019-07-02 Investigating the properties of TBA variants with twin thrombin binding domains Amato, Teresa Virgilio, Antonella Pirone, Luciano Vellecco, Valentina Bucci, Mariarosaria Pedone, Emilia Esposito, Veronica Galeone, Aldo Sci Rep Article In this paper, we report studies concerning thrombin binding aptamer (TBA) dimeric derivatives in which the 3′-ends of two TBA sequences have been joined by means of linkers containing adenosine or thymidine residues and/or a glycerol moiety. CD and electrophoretic investigations indicate that all modified aptamers are able to form G-quadruplex domains resembling that of the parent TBA structure. However, isothermal titration calorimetry measurements of the aptamer/thrombin interaction point to different affinities to the target protein, depending on the type of linker. Consistently, the best ligands for thrombin show anticoagulant activities higher than TBA. Interestingly, two dimeric aptamers with the most promising properties also show far higher resistances in biological environment than TBA. Nature Publishing Group UK 2019-06-24 /pmc/articles/PMC6591170/ /pubmed/31235717 http://dx.doi.org/10.1038/s41598-019-45526-z Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Amato, Teresa
Virgilio, Antonella
Pirone, Luciano
Vellecco, Valentina
Bucci, Mariarosaria
Pedone, Emilia
Esposito, Veronica
Galeone, Aldo
Investigating the properties of TBA variants with twin thrombin binding domains
title Investigating the properties of TBA variants with twin thrombin binding domains
title_full Investigating the properties of TBA variants with twin thrombin binding domains
title_fullStr Investigating the properties of TBA variants with twin thrombin binding domains
title_full_unstemmed Investigating the properties of TBA variants with twin thrombin binding domains
title_short Investigating the properties of TBA variants with twin thrombin binding domains
title_sort investigating the properties of tba variants with twin thrombin binding domains
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6591170/
https://www.ncbi.nlm.nih.gov/pubmed/31235717
http://dx.doi.org/10.1038/s41598-019-45526-z
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