ArticleNature nanotechnology2025
Evolution of multivalent supramolecular assemblies of aptamers with target-defined spatial organization.
Article in Nature nanotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Multivalent Aptamers: Contemporary Engineering Strategies and Biomedical Applications.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
- Stability modification of therapeutic aptamers: from biostability bottlenecks to nuclease-resistant construct design.RSC chemical biology · 2026Review
- Fluorescent covalent organic framework and multivalent aptamer-driven magnetic nanoplatform for sensitive detection of foodborne pathogens.Mikrochimica acta · 2026Article
- A general strategy to enhance aptamer affinity by suppressing dissociation through symmetric assembly.Nucleic acids research · 2026Article
- Evolution of Multivalent Aptamer Corona for High-Throughput Multiplexed Detection of Multiple Cancers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Selection and Characterization of SARS-CoV-2 Spike Binding Clickmers.Chembiochem : a European journal of chemical biology · 2026Article
- Y-shaped trivalent aptamer for targeted visualization and tracking of reprogrammed astrocytes.Materials today. Bio · 2025Article
- Evolution of multivalent supramolecular assemblies of aptamers with target-defined spatial organization.Nature nanotechnology · 2025Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Rapid identification of neutralizing molecules against new and mutating viruses is key to efficiently combating biorisk. Current binder identification techniques use a monovalent library of potential binders. Interestingly, proteins on pathogens are often homo-oligomeric-for example, the SARS-CoV-2 spike protein is a homotrimer. Here we describe a simple strategy, MEDUSA (multivalent evolved DNA-based supramolecular assembly), to evolve multivalent assemblies of aptamers with precise interligand spacing and three-fold symmetry, mirroring the geometric structure of many viral capsid proteins. MEDUSA allowed the selection of potent SARS-CoV-2 spike binders structurally distinct from any known aptamers. Decoupling the geometric and structural rigidity contributions toward selectivity made it possible to connect form to function, as demonstrated by the design of tunable fluorescent sensors. This approach offers a blueprint for targeting geometrically defined pathogen structures and developing rapid-response tools for emerging pathogens.
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Registered trials
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