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Biophys. J. BioFAST: First Published September 22, 2006. doi:10.1529/biophysj.106.090449
© 2006 by the Biophysical Society.

A more recent version of this article appeared on December 1, 2006.
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Martijn E. van Raaij
Ine M. J. Segers-Nolten
Vinod Subramaniam
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SPECTROSCOPY, IMAGING, OTHER TECHNIQUES

Quantitative morphological analysis reveals ultrastructural diversity of amyloid fibrils from {alpha}-synuclein mutants

Martijn E. van Raaij 1, Ine M. J. Segers-Nolten 1 and Vinod Subramaniam 1*

1 University of Twente

* To whom correspondence should be addressed. E-mail: v.subramaniam{at}tnw.utwente.nl.

Submitted on June 2, 2006
Revised on July 26, 2006
Accepted on 5 September 2006


  Abstract
High resolution atomic force microscopy is a powerful tool to characterize nanoscale morphological features of protein amyloid fibrils. Comparison of fibril morphological properties between studies has been hampered by differences in analysis procedures and measurement error determination used by various authors. We describe a fibril morphology analysis method that allows for quantitative comparison of features of amyloid fibrils of any amyloidogenic protein measured by atomic force microscopy. We have used tapping mode atomic force microscopy in liquid to measure the morphology of fibrillar aggregates of human wildtype {alpha}-synuclein and the disease-related mutants A30P, E46K and A53T. Analysis of the images shows that fibrillar aggregates formed by E46K {alpha}-synuclein have a smaller diameter (9.0 ± 0.8 nm) and periodicity (mode at 55 nm) than fibrils of wildtype {alpha}-synuclein (height 10.0 ± 1.1 nm, periodicity has a mode at 65 nm). Fibrils of A30P have smaller diameter still (8.1 ± 1.2 nm) and show a variety of periodicities. This quantitative analysis procedure enables comparison of the results with existing models for assembly of amyloid fibrils.

Key Words: alpha-synuclein, atomic force microsocpy, fibril, quantitative analysis, ultrastructure




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Copyright © 2006 by the Biophysical Society.