Xue, WF, Homans, SW and Radford, SE (2009) Amyloid fibril length distribution quantified by atomic force microscopy single-particle image analysis. Protein Engineering Design and Selection, 22 (8). 489 - 496. ISSN 1741-0126
Abstract
Amyloid fibrils are proteinaceous nano-scale linear aggregates. They are of key interest not only because of their association with numerous disorders, such as type II diabetes mellitus, Alzheimer's and Parkinson's diseases, but also because of their potential to become engineered high-performance nano-materials. Methods to characterise the length distribution of nano-scale linear aggregates such as amyloid fibrils are of paramount importance both in understanding the biological impact of these aggregates and in controlling their mechanical properties as potential nano-materials. Here, we present a new quantitative approach to the determination of the length distribution of amyloid fibrils using tapping-mode atomic force microscopy. The method described employs single-particle image analysis corrected for the length-dependent bias that is a common problem associated with surface-based imaging techniques. Applying this method, we provide a detailed characterisation of the length distribution of samples containing long-straight fibrils formed in vitro from β2-microglobulin. The results suggest that the Weibull distribution is a suitable model in describing fibril length distributions, and reveal that fibril fragmentation is an important process even under unagitated conditions. These results demonstrate the significance of quantitative length distribution measurements in providing important new information regarding amyloid assembly.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2009 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
Keywords: | Bias correction; Brittleness; Fibril fragmentation; Single-molecule method; Size distribution; Protein Aggregation; Beta(2)-Microglobulin; Dependence |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 21 Apr 2015 08:57 |
Last Modified: | 15 Oct 2019 15:15 |
Published Version: | http://dx.doi.org/10.1093/protein/gzp026 |
Status: | Published |
Publisher: | Oxford University Press (OUP) |
Identification Number: | 10.1093/protein/gzp026 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:84064 |