Nanopore analysis of amyloid fibrils formed by lysozyme aggregation
Royal Society of Chemistry
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Martyushenko, N., Bell, N., Lamboll, R., & Keyser, U. (2015). Nanopore analysis of amyloid fibrils formed by lysozyme aggregation. Analyst, 140 4882-4886. https://doi.org/10.1039/C5AN00530B
The measurement of single particle size distributions of amyloid fibrils is crucial for determining mechanisms of growth and toxicity. Nanopore sensing is an attractive solution for this problem since it gives information on aggregates’ shapes with relatively high throughput for a single particle technology. In this paper we study the translocation of lysozyme fibrils through quartz glass nanopores. We demonstrate that, under appropriate salt and pH conditions, lysozyme fibrils translocate through bare quartz nanopores without causing significant clogging. This enables us to measure statistics on tens of thousands of translocations of lysozyme fibrils with the same nanopore and track their development over a time course of aggregation spanning 24h. Analysis of our events shows that the statistics are consistent with a simple bulk conductivity model for the passage of rods with a fixed cross sectional area through a conical glass nanopore.
N.A.W.B. acknowledges funding from the EPSRC NanoDTC program and an EPSRC doctoral prize award and U.F.K. acknowledges funding from an ERC starting grant, PassMembrane (261101).
European Research Council (261101)
External DOI: https://doi.org/10.1039/C5AN00530B
This record's URL: https://www.repository.cam.ac.uk/handle/1810/248809
Licence URL: http://creativecommons.org/licenses/by/4.0/