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Detecting Selective Protein Binding Inside Plasmonic Nanopores: Toward a Mimic of the Nuclear Pore Complex
Biosensors based on plasmonic nanostructures offer label-free and real-time monitoring of biomolecular interactions. However, so do many other surface sensitive techniques with equal or better resolution in terms of surface coverage. Yet, plasmonic nanostructures offer unique possibilities to study...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6308133/ https://www.ncbi.nlm.nih.gov/pubmed/30619840 http://dx.doi.org/10.3389/fchem.2018.00637 |
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author | Malekian, Bita Schoch, Rafael L. Robson, Timothy Ferrand -Drake del Castillo, Gustav Xiong, Kunli Emilsson, Gustav Kapinos, Larisa E. Lim, Roderick Y. H. Dahlin, Andreas |
author_facet | Malekian, Bita Schoch, Rafael L. Robson, Timothy Ferrand -Drake del Castillo, Gustav Xiong, Kunli Emilsson, Gustav Kapinos, Larisa E. Lim, Roderick Y. H. Dahlin, Andreas |
author_sort | Malekian, Bita |
collection | PubMed |
description | Biosensors based on plasmonic nanostructures offer label-free and real-time monitoring of biomolecular interactions. However, so do many other surface sensitive techniques with equal or better resolution in terms of surface coverage. Yet, plasmonic nanostructures offer unique possibilities to study effects associated with nanoscale geometry. In this work we use plasmonic nanopores with double gold films and detect binding of proteins inside them. By thiol and trietoxysilane chemistry, receptors are selectively positioned on the silicon nitride interior walls. Larger (~150 nm) nanopores are used detect binding of averaged sized proteins (~60 kg/mol) with high signal to noise (>100). Further, we fabricate pores that approach the size of the nuclear pore complex (diameter down to 50 nm) and graft disordered phenylalanine-glycine nucleoporin domains to the walls, followed by titration of karyopherinβ1 transport receptors. The interactions are shown to occur with similar affinity as determined by conventional surface plasmon resonance on planar surfaces. Our work illustrates another unique application of plasmonic nanostructures, namely the possibility to mimic the geometry of a biological nanomachine with integrated optical sensing capabilities. |
format | Online Article Text |
id | pubmed-6308133 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-63081332019-01-07 Detecting Selective Protein Binding Inside Plasmonic Nanopores: Toward a Mimic of the Nuclear Pore Complex Malekian, Bita Schoch, Rafael L. Robson, Timothy Ferrand -Drake del Castillo, Gustav Xiong, Kunli Emilsson, Gustav Kapinos, Larisa E. Lim, Roderick Y. H. Dahlin, Andreas Front Chem Chemistry Biosensors based on plasmonic nanostructures offer label-free and real-time monitoring of biomolecular interactions. However, so do many other surface sensitive techniques with equal or better resolution in terms of surface coverage. Yet, plasmonic nanostructures offer unique possibilities to study effects associated with nanoscale geometry. In this work we use plasmonic nanopores with double gold films and detect binding of proteins inside them. By thiol and trietoxysilane chemistry, receptors are selectively positioned on the silicon nitride interior walls. Larger (~150 nm) nanopores are used detect binding of averaged sized proteins (~60 kg/mol) with high signal to noise (>100). Further, we fabricate pores that approach the size of the nuclear pore complex (diameter down to 50 nm) and graft disordered phenylalanine-glycine nucleoporin domains to the walls, followed by titration of karyopherinβ1 transport receptors. The interactions are shown to occur with similar affinity as determined by conventional surface plasmon resonance on planar surfaces. Our work illustrates another unique application of plasmonic nanostructures, namely the possibility to mimic the geometry of a biological nanomachine with integrated optical sensing capabilities. Frontiers Media S.A. 2018-12-21 /pmc/articles/PMC6308133/ /pubmed/30619840 http://dx.doi.org/10.3389/fchem.2018.00637 Text en Copyright © 2018 Malekian, Schoch, Robson, Ferrand -Drake del Castillo, Xiong, Emilsson, Kapinos, Lim and Dahlin. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Chemistry Malekian, Bita Schoch, Rafael L. Robson, Timothy Ferrand -Drake del Castillo, Gustav Xiong, Kunli Emilsson, Gustav Kapinos, Larisa E. Lim, Roderick Y. H. Dahlin, Andreas Detecting Selective Protein Binding Inside Plasmonic Nanopores: Toward a Mimic of the Nuclear Pore Complex |
title | Detecting Selective Protein Binding Inside Plasmonic Nanopores: Toward a Mimic of the Nuclear Pore Complex |
title_full | Detecting Selective Protein Binding Inside Plasmonic Nanopores: Toward a Mimic of the Nuclear Pore Complex |
title_fullStr | Detecting Selective Protein Binding Inside Plasmonic Nanopores: Toward a Mimic of the Nuclear Pore Complex |
title_full_unstemmed | Detecting Selective Protein Binding Inside Plasmonic Nanopores: Toward a Mimic of the Nuclear Pore Complex |
title_short | Detecting Selective Protein Binding Inside Plasmonic Nanopores: Toward a Mimic of the Nuclear Pore Complex |
title_sort | detecting selective protein binding inside plasmonic nanopores: toward a mimic of the nuclear pore complex |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6308133/ https://www.ncbi.nlm.nih.gov/pubmed/30619840 http://dx.doi.org/10.3389/fchem.2018.00637 |
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