ArticleNature communications2023
Stable trapping of multiple proteins at physiological conditions using nanoscale chambers with macromolecular gates.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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
7 citing papers in PubMed.
- A Nanopore-Gated Subattoliter Silicon Nanocavity for Single-Molecule Trapping and Analysis without Applying an External Force.ACS nano · 2026Article
- Research progress and application of solid-state nanopore fabrication based on wet etching.Fundamental research · 2026Review
- Elucidating the nanoscopic organization and dynamics of the nuclear pore complex.Nucleus (Austin, Tex.) · 2025Article
- Responsive Polyelectrolyte Brushes in Applications: Functions, Stimuli, and Design Considerations.Advanced materials (Deerfield Beach, Fla.) · 2025Review
- The Emergence of Nanofluidics for Single-Biomolecule Manipulation and Sensing.Analytical chemistry · 2025Review
- Coacervate-pore complexes for selective molecular transport and dynamic reconfiguration.Nature communications · 2024Article
- Interactive biocatalysis achieved by driving enzyme cascades inside a porous conducting material.Communications chemistry · 2024Review
Corrections and comments
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Authors and funding
13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The possibility to detect and analyze single or few biological molecules is very important for understanding interactions and reaction mechanisms. Ideally, the molecules should be confined to a nanoscale volume so that the observation time by optical methods can be extended. However, it has proven difficult to develop reliable, non-invasive trapping techniques for biomolecules under physiological conditions. Here we present a platform for long-term tether-free (solution phase) trapping of proteins without exposing them to any field gradient forces. We show that a responsive polymer brush can make solid state nanopores switch between a fully open and a fully closed state with respect to proteins, while always allowing the passage of solvent, ions and small molecules. This makes it possible to trap a very high number of proteins (500-1000) inside nanoscale chambers as small as one attoliter, reaching concentrations up to 60 gL
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Registered trials
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