FIB-milled plasmonic nanoapertures allow for long trapping times of individual proteins

Wayne Yang, Madeleine van Dijk, Christian Primavera, Cees Dekker*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

6 Citations (Scopus)
2 Downloads (Pure)

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.

Original languageEnglish
Article number103237
Number of pages14
JournaliScience
Volume24
Issue number11
DOIs
Publication statusPublished - 2021

Keywords

  • Biophysical chemistry
  • Materials science
  • Physical chemistry
  • Protein

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