An Analytical Solution to the Kinetics of Breakable Filament Assembly

Author:

Knowles Tuomas P. J.12,Waudby Christopher A.3,Devlin Glyn L.3,Cohen Samuel I. A.3,Aguzzi Adriano4,Vendruscolo Michele3,Terentjev Eugene M.1,Welland Mark E.2,Dobson Christopher M.3

Affiliation:

1. Cavendish Laboratory, University of Cambridge, J. J. Thomson Avenue, Cambridge CB3 0HE, UK.

2. Nanoscience Centre, University of Cambridge, J. J. Thomson Avenue, Cambridge CB3 0FF, UK.

3. Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.

4. Institute of Neuropathology, University Hospital Zurich, Schmelzbergstrasse, 8091 Zurich, Switzerland.

Abstract

Dissecting Amyloid Formation Amyloid fibrils are associated with clinical disorders ranging from Alzheimer's disease to type II diabetes. Their self-assembly can be described by a master equation that takes into account nucleation-dependent polymerization and fragmentation. Knowles et al. (p. 1533 ) now present an analytical solution to the master equation, which shows that amyloid growth kinetics is often limited by the fragmentation rate rather than by the rate of primary nucleation. In addition, the results reveal relationships between system properties (scaling laws) that provide mechanistic insight not only into amyloid growth, but also into related self-assembly processes.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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