TY - JOUR
T1 - FIB-milled plasmonic nanoapertures allow for long trapping times of individual proteins
AU - Yang, Wayne
AU - van Dijk, Madeleine
AU - Primavera, Christian
AU - Dekker, Cees
PY - 2021
Y1 - 2021
N2 - 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.
AB - 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.
KW - Biophysical chemistry
KW - Materials science
KW - Physical chemistry
KW - Protein
UR - http://www.scopus.com/inward/record.url?scp=85122723056&partnerID=8YFLogxK
U2 - 10.1016/j.isci.2021.103237
DO - 10.1016/j.isci.2021.103237
M3 - Article
AN - SCOPUS:85122723056
SN - 2589-0042
VL - 24
JO - iScience
JF - iScience
IS - 11
M1 - 103237
ER -