ArticleScience advances2025
Decoding aptamer-protein binding kinetics for continuous biosensing using single-molecule techniques.
Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Nucleic acid aptamers: new methods for selection, target validation, molecular diagnostics and therapeutics.Signal transduction and targeted therapy · 2026Review
- Beyond Detection Limits: Integrated Biosensors for Molecular Diagnostics, Longitudinal Monitoring, and Clinical Translation.Biosensors · 2026Review
- Molecularly Imprinted Polymers for Biosensing: From Synthetic Recognition to Integrated Biointerfaces.Micromachines · 2026Review
- A pressure-tolerant, miniature ocean-sensing tag with acoustic telemetry for real-time CTD monitoring.Science advances · 2026Article
- Twist-encoded magnetic plasmon interferometry for label-free, orientation-resolved single-molecule imaging.Science advances · 2026Article
- Massive barcode-free chemical screenings enable the discovery of bioactive macrocycles with passive membrane permeability.Nature communications · 2026Article
- Article
- Designing the Future of Biosensing: Advances in Aptamer Discovery, Computational Modeling, and Diagnostic Applications.Biosensors · 2025Review
- Single-Molecule Protein Interactions and Unfolding Revealed by Plasmon-Enhanced Fluorescence.Analytical chemistry · 2025Article
- Photoactivatable Aptamer-Based Biosensors for Point-of-Care Testing: Advances and Applications.Biosensors · 2025Review
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Continuous biosensing provides real-time information about biochemical processes and holds great potential for health monitoring. Aptamers have emerged as promising alternatives over traditional biorecognition elements. However, the underlying aptamer-target binding interactions are often poorly understood. Here, we present a technique that can decode aptamer-protein binding interactions at the single-molecule level. We demonstrate that our single-molecule assay is able to decode the underlying binding kinetics of aptamers despite their similar binding affinity. Guided by computational simulations and validated with quartz crystal microbalance experiments, we show that the quantitative insights generated by this single-molecule technique enabled the rational understanding of biosensor performance (i.e., the sensitivity and limit of detection). This capability was demonstrated with thrombin as the analyte and the structurally similar aptamers HD1, RE31, and NU172 as the biorecognition elements. This work decodes aptamer-protein interactions with high temporal resolution, paving the way for the rational design of aptamer-based biosensors.
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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.