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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Bibliographic Details
Published in:Scientific reports 2019-06, Vol.9 (1), p.9184-8, Article 9184
Main Authors: Amato, Teresa, Virgilio, Antonella, Pirone, Luciano, Vellecco, Valentina, Bucci, Mariarosaria, Pedone, Emilia, Esposito, Veronica, Galeone, Aldo
Format: Article
Language:English
Subjects:
631/337
631/92/147
Adenosine
Annealing
Anticoagulants
Antithrombins - chemistry
Aptamers
Aptamers, Nucleotide - chemistry
Calorimetry
G-Quadruplexes
Glycerol
Humanities and Social Sciences
Investigations
Ligands
Models, Molecular
multidisciplinary
Protein Binding
Science
Science (multidisciplinary)
Thrombin
Thrombin - chemistry
Thymidine
Titration
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Summary: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.
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-019-45526-z