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Issue 14, 2015
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Nanopore analysis of amyloid fibrils formed by lysozyme aggregation

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Abstract

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 24 h. 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.

Graphical abstract: Nanopore analysis of amyloid fibrils formed by lysozyme aggregation

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Publication details

The article was received on 17 Mar 2015, accepted on 12 May 2015 and first published on 12 May 2015


Article type: Paper
DOI: 10.1039/C5AN00530B
Citation: Analyst, 2015,140, 4882-4886
  • Open access: Creative Commons BY license
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    Nanopore analysis of amyloid fibrils formed by lysozyme aggregation

    N. Martyushenko, N. A. W. Bell, R. D. Lamboll and U. F. Keyser, Analyst, 2015, 140, 4882
    DOI: 10.1039/C5AN00530B

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