ArticleScience advances2022
The role of DNA nanostructures in the catalytic properties of an allosterically regulated protease.
Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The trial behind it
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Who cites it
11 citing papers in PubMed.
- DNA-Enzyme Hybrid Nanostructures: Functional Materials to Modulate Enzymatic Activity.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
- Recent Advances in Aptamer-Based Applications in Cardiology.International journal of molecular sciences · 2026Review
- Current Progress and Future Directions of Enzyme Technology in Food Nutrition: A Comprehensive Review of Processing, Nutrition, and Functional Innovation.Foods (Basel, Switzerland) · 2026Review
- Reaction Engineering of In Vitro Natural Product Biosynthesis: Challenges and Strategies.Chembiochem : a European journal of chemical biology · 2025Review
- A Computational Perspective to Intermolecular Interactions and the Role of the Solvent on Regulating Protein Properties.Chemical reviews · 2025Review
- Isothermal assembly of DNA nanostructures.Chemical communications (Cambridge, England) · 2025Review
- Enzyme Reactions Are Accelerated or Decelerated When the Enzymes Are Located Near the DNA Nanostructure.ACS applied materials & interfaces · 2025Article
- Precise construction of DNA origami-based materials for functional regulation on biological interface.Smart molecules : open access · 2024Review
- Customized Scaffolds for Direct Assembly of Functionalized DNA Origami.ACS applied materials & interfaces · 2023Article
- Recent Advances in DNA Origami-Engineered Nanomaterials and Applications.Chemical reviews · 2023Review
- Mechanistic Aspects for the Modulation of Enzyme Reactions on the DNA Scaffold.Molecules (Basel, Switzerland) · 2022Review
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA-scaffolded enzymes typically show altered kinetic properties; however, the mechanism behind this phenomenon is still poorly understood. We address this question using thrombin, a model of allosterically regulated serine proteases, encaged into DNA origami cavities with distinct structural and electrostatic features. We compare the hydrolysis of substrates that differ only in their net charge due to a terminal residue far from the cleavage site and presumably involved in the allosteric activation of thrombin. Our data show that the reaction rate is affected by DNA/substrate electrostatic interactions, proportionally to the degree of DNA/enzyme tethering. For substrates of opposite net charge, this leads to an inversion of the catalytic response of the DNA-scaffolded thrombin when compared to its freely diffusing counterpart. Hence, by altering the electrostatic environment nearby the encaged enzyme, DNA nanostructures interfere with charge-dependent mechanisms of enzyme-substrate recognition and may offer an alternative tool to regulate allosteric processes through spatial confinement.
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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.