Stable trapping of multiple proteins at physiological conditions using nanoscale chambers with macromolecular gates

Justas Svirelis, Zeynep Adali, Gustav Emilsson, Jesper Medin, John Andersson, Radhika Vattikunta, Mats Hulander, Julia Järlebark, Krzysztof Kolman, Oliver Olsson, Yusuke Sakiyama, Roderick Y. H. Lim and Andreas Dahlin ()
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Justas Svirelis: Chalmers University of Technology
Zeynep Adali: Chalmers University of Technology
Gustav Emilsson: Chalmers University of Technology
Jesper Medin: Chalmers University of Technology
John Andersson: Chalmers University of Technology
Radhika Vattikunta: Chalmers University of Technology
Mats Hulander: Chalmers University of Technology
Julia Järlebark: Chalmers University of Technology
Krzysztof Kolman: Chalmers University of Technology
Oliver Olsson: Chalmers University of Technology
Yusuke Sakiyama: University of Basel
Roderick Y. H. Lim: University of Basel
Andreas Dahlin: Chalmers University of Technology

Nature Communications, 2023, vol. 14, issue 1, 1-14

Abstract: 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−1. Our method is fully compatible with parallelization by imaging arrays of nanochambers. Additionally, we show that enzymatic cascade reactions can be performed with multiple native enzymes under full nanoscale confinement and steady supply of reactants. This platform will greatly extend the possibilities to optically analyze interactions involving multiple proteins, such as the dynamics of oligomerization events.

Date: 2023
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DOI: 10.1038/s41467-023-40889-4

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