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Quantitative approaches for characterising fibrillar protein nanostructures

Published online by Cambridge University Press:  01 February 2011

Tuomas P. J. Knowles
Affiliation:
tpjk2@cam.ac.ukUniversity of CambridgeDepartment of Chemistry, Cambridge, United Kingdom
Duncan A. White
Affiliation:
daw64@cam.ac.ukUniversity of CambridgeDepartment of Chemistry, Cambridge, Cambridgeshire, United Kingdom
Christopher M. Dobson
Affiliation:
cmd44@cam.ac.ukUniversity of CambridgeDepartment of Chemistry, Cambridge, Cambridgeshire, United Kingdom
Mark E. Welland
Affiliation:
mew10@cam.ac.ukUniversity of CambridgeNanoscience Centre, Cambridge, Cambridgeshire, United Kingdom
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Abstract

Polypeptide sequences have an inherent tendency to self-assemble into filamentous nanostructures commonly known as amyloid fibrils. Such self-assembly is used in nature to generate a variety of functional materials ranging from protective coatings in bacteria to catalytic scaffolds in mammals. The aberrant self-assembly of misfolded peptides and proteins is also, however, implicated in a range of disease states including neurodegenerative conditions such as Alzheimer's and Parkinson's diseases. It is increasingly evident that the intrinsic material properties of these structures are crucial for understanding the thermodynamics and kinetics of the pathological deposition of proteins, particularly as the mechanical fragmentation of aggregates enhances the rate of protein deposition by exposing new fibril ends which can promote further growth. We discuss here recent advances in physical techniques that are able to characterise the hierarchical self-assembly of misfolded protein molecules and define their properties.

Type
Research Article
Copyright
Copyright © Materials Research Society 2010

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