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Single-molecule nanopore sensing of actin dynamics and drug binding

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Abstract

Actin is a key protein in the dynamic processes within the eukaryotic cell. To date, methods exploring the molecular state of actin are limited to insights gained from structural approaches, providing a snapshot of protein folding, or methods that require chemical modifications compromising actin monomer thermostability. Nanopore sensing permits label-free investigation of native proteins and is ideally suited to study proteins such as actin that require specialised buffers and cofactors. Using nanopores, we determined the state of actin at the macromolecular level (filamentous or globular) and in its monomeric form bound to inhibitors. We revealed urea-dependent and voltage-dependent transitional states and observed the unfolding process within which sub-populations of transient actin oligomers are visible. We detected, in real-time, filament-growth, and drug-binding at the single-molecule level demonstrating the promise of nanopore sensing for in-depth understanding of protein folding landscapes and for drug discovery.

Graphical abstract: Single-molecule nanopore sensing of actin dynamics and drug binding

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Publication details

The article was received on 11 Nov 2019, accepted on 02 Dec 2019 and first published on 03 Dec 2019


Article type: Edge Article
DOI: 10.1039/C9SC05710B
Chem. Sci., 2020, Advance Article
  • Open access: Creative Commons BY license
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    Single-molecule nanopore sensing of actin dynamics and drug binding

    X. Wang, M. D. Wilkinson, X. Lin, R. Ren, K. R. Willison, A. P. Ivanov, J. Baum and J. B. Edel, Chem. Sci., 2020, Advance Article , DOI: 10.1039/C9SC05710B

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