ArticleiScience2021
FIB-milled plasmonic nanoapertures allow for long trapping times of individual proteins.
Article in iScience, 2021. 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.
- Plasmonic Optical Tweezers and Surface-Enhanced Raman Spectroscopy: Fundamentals, Single-Entity Applications, and the Evolving Role of Artificial Intelligence.Bioengineering (Basel, Switzerland) · 2026Review
- Label-Free Single-Molecule Conalbumin Analysis.Micromachines · 2026Article
- Surface-Enhanced Raman Spectroscopy for Biomedical Applications: Recent Advances and Future Challenges.ACS applied materials & interfaces · 2025Review
- Direct observation of small molecule activator binding to single PR65 protein.Npj biosensing · 2025Article
- Influence of point mutations on PR65 conformational adaptability: Insights from molecular simulations and nanoaperture optical tweezers.Science advances · 2024Article
- Thermometric Analysis of Nanoaperture-Trapped Erbium-Containing Nanocrystals.ACS photonics · 2024Article
- Energy landscape of conformational changes for a single unmodified protein.Npj biosensing · 2024Article
- Single molecule DNA origami nanoarrays with controlled protein orientation.Biophysics reviews · 2022Article
- Review
- Enhanced Optical Spectroscopy for Multiplexed DNA and Protein-Sequencing with Plasmonic Nanopores: Challenges and Prospects.Analytical chemistry · 2022Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have developed a fabrication methodology for label-free optical trapping of individual nanobeads and proteins in inverted-bowtie-shaped plasmonic gold nanopores. Arrays of these nanoapertures can be reliably produced using focused ion beam (FIB) milling with gap sizes of 10-20 nm, single-nanometer variation, and with a remarkable stability that allows for repeated use. We employ an optical readout where the presence of the protein entering the trap is marked by an increase in the transmission of light through the nanoaperture from the shift of the plasmonic resonance. In addition, the optical trapping force of the plasmonic nanopores allows 20-nm polystyrene beads and proteins, such as beta-amylase and Heat Shock Protein (HSP90), to be trapped for very long times (approximately minutes). On demand, we can release the trapped molecule for another protein to be interrogated. Our work opens up new routes to acquire information on the conformation and dynamics of individual proteins.
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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 Socratic graph.