ArticleScientific reports2019
Investigating the properties of TBA variants with twin thrombin binding domains.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 47 citations in OpenAlex.
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- Generation of single stranded DNA with selective affinity to bovine spermatozoa.Animal bioscience · 2021Article
- Beyond G-Quadruplexes-The Effect of Junction with Additional Structural Motifs on Aptamers Properties.International journal of molecular sciences · 2021Review
- Overview of the Therapeutic Potential of Aptamers Targeting Coagulation Factors.International journal of molecular sciences · 2021Review
- Covalent Bi-Modular Parallel and Antiparallel G-Quadruplex DNA Nanocostructs Reduce Viability of Patient Glioma Primary Cell Cultures.International journal of molecular sciences · 2021Article
- Dimeric and Multimeric DNA Aptamers for Highly Effective Protein Recognition.Molecules (Basel, Switzerland) · 2020Review
- Tuning the Polymorphism of the Anti-VEGF G-rich V7t1 Aptamer by Covalent Dimeric Constructs.International journal of molecular sciences · 2020Article
- Aptamers Chemistry: Chemical Modifications and Conjugation Strategies.Molecules (Basel, Switzerland) · 2019Review
- G-Quadruplex-Forming Aptamers-Characteristics, Applications, and Perspectives.Molecules (Basel, Switzerland) · 2019Review
- Bimodular Antiparallel G-Quadruplex Nanoconstruct with Antiproliferative Activity.Molecules (Basel, Switzerland) · 2019Article
- A Mini-Review: Clinical Development and Potential of Aptamers for Thrombotic Events Treatment and Monitoring.Biomedicines · 2019Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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