ArticleNucleic acids research2017
Through-bond effects in the ternary complexes of thrombin sandwiched by two DNA aptamers.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 74 citations in OpenAlex.
- Protein-protein interaction disruption as a next-generation antithrombotic strategy.Journal of thrombosis and thrombolysis · 2026Review
- Retention-Based, Dissociation-Sensitive Pre-Screening of Aptamers Using a Centrifugal Microspin Filter.Biosensors · 2026Article
- Possible Thrombus-clearing Mechanism and Modification Suggestion of β-sitosterol.Current drug targets · 2026Article
- Design and Evaluation of Sticky End-Type Bivalent DNA Aptamers Containing M08s-1 as Anticoagulant Agents.ChemMedChem · 2025Article
- Single-Molecule DNA Tweezers Enable Programmable Control of Enzyme Activity via Arbitrary Molecular Cues.Angewandte Chemie (International ed. in English) · 2025Article
- Unlocking precision in aptamer engineering: a case study of the thrombin binding aptamer illustrates why modification size, quantity, and position matter.Nucleic acids research · 2024Article
- Aptamer-Based DNA Allosteric Switch for Regulation of Protein Activity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Aptameric hirudins as selective and reversible EXosite-ACTive site (EXACT) inhibitors.Nature communications · 2024Article
- Structural Insights into Protein-Aptamer Recognitions Emerged from Experimental and Computational Studies.International journal of molecular sciences · 2023Review
- A neutralizable dimeric anti-thrombin aptamer with potent anticoagulant activity in mice.Molecular therapy. Nucleic acids · 2023Article
- ASC-G4, an algorithm to calculate advanced structural characteristics of G-quadruplexes.Nucleic acids research · 2023Article
- Analytical Perspectives in the Study of Polyvalent Interactions of Free and Surface-Bound Oligonucleotides and Their Implications in Affinity Biosensing.International journal of molecular sciences · 2022Article
- A terminal functionalization strategy reveals unusual binding abilities of anti-thrombin anticoagulant aptamers.Molecular therapy. Nucleic acids · 2022Article
- Advances in Aptamers-Based Applications in Breast Cancer: Drug Delivery, Therapeutics, and Diagnostics.International journal of molecular sciences · 2022Review
- Calibrating Catalytic DNA Nanostructures for Site-Selective Protein Modification.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Exosite Binding in Thrombin: A Global Structural/Dynamic Overview of Complexes with Aptamers and Other Ligands.International journal of molecular sciences · 2021Review
- Design strategy of antidote sequence for bivalent aptamer: Rapid neutralization of high-anticoagulant thrombin-binding bivalent DNA aptamer-linked M08 with HD22.Research and practice in thrombosis and haemostasis · 2021Article
- Structural Biology for the Molecular Insight between Aptamers and Target Proteins.International journal of molecular sciences · 2021Review
- Aptamer-Functionalized Natural Protein-Based Polymers as Innovative Biomaterials.Pharmaceutics · 2020Review
- Site-Specific and Trigger-Activated Modification of Proteins by Means of Catalytic Hemin/G-quadruplex DNAzyme Nanostructures.Bioconjugate chemistry · 2020Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aptamers directed against human thrombin can selectively bind to two different exosites on the protein surface. The simultaneous use of two DNA aptamers, HD1 and HD22, directed to exosite I and exosite II respectively, is a very powerful approach to exploit their combined affinity. Indeed, strategies to link HD1 and HD22 together have been proposed in order to create a single bivalent molecule with an enhanced ability to control thrombin activity. In this work, the crystal structures of two ternary complexes, in which thrombin is sandwiched between two DNA aptamers, are presented and discussed. The structures shed light on the cross talk between the two exosites. The through-bond effects are particularly evident at exosite II, with net consequences on the HD22 structure. Moreover, thermodynamic data on the binding of the two aptamers are also reported and analyzed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.