Nanopore analysis of amyloid fibrils formed by lysozyme aggregation. Issue 14 (21st May 2015)

• Record Type: Journal Article
• Authors: Martyushenko, Nikolay; Bell, Nicholas A. W.; Lamboll, Robin D.; Keyser, Ulrich F.
• Is Part Of: Analyst. Volume 140:Issue 14(2015)
• Page Start: 4882
• Page End: 4886
• Publication Date: 2015-05-21
• Subjects: Chemistry, Analytic -- Periodicals; 543
• DOI: 10.1039/c5an00530b
• Languages: English
• ISSNs: 0003-2654

Abstract

Abstract : Lysozyme fibrils translocate uncoated glass nanopores at low pH without significant non-specific sticking enabling unprecedented statistics on thousands of fibril translocations and comparison with a simple bulk conductivity model. 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.