Skip to main content

Amyloid fibril length distribution quantified by atomic force microscopy single-particle image analysis

Xue, Wei-Feng, Homans, Steve W., Radford, Sheena E. (2009) Amyloid fibril length distribution quantified by atomic force microscopy single-particle image analysis. Protein Engineering Design and Selection, 22 (8). pp. 489-496. ISSN 1741-0126. (doi:10.1093/protein/gzp026) (KAR id:31443)

PDF Publisher pdf
Language: English
Download (424kB) Preview
[thumbnail of Xue et al PEDS (2009) 22 489.pdf]
This file may not be suitable for users of assistive technology.
Request an accessible format
Official URL


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 ?2-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

Item Type: Article
DOI/Identification number: 10.1093/protein/gzp026
Uncontrolled keywords: bias correction; brittleness; fibril fragmentation; single-molecule method; size distribution
Subjects: Q Science
Q Science > QC Physics
Q Science > QD Chemistry
Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Divisions > Division of Natural Sciences > School of Biosciences
Depositing User: Wei-Feng Xue
Date Deposited: 09 Oct 2012 13:18 UTC
Last Modified: 01 Aug 2019 10:35 UTC
Resource URI: (The current URI for this page, for reference purposes)
Xue, Wei-Feng:
  • Depositors only (login required):


Downloads per month over past year