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Kinetics and thermodynamics of amyloid fibril assembly.

Wetzel R

Graduate School of Medicine, University of Tennessee, 1924 Alcoa Highway, Knoxville, Tennessee 37920, USA.

With some exceptions, amyloids appear to be accidental aggregated structures whose formation was not selected for in molecular evolution. Despite this, amyloid fibrils are in many respects surprisingly well-behaved molecules. For example, Huntington's disease-related polyglutamine sequences aggregate via a relatively simple nucleated growth polymerization mechanism. In addition, the Alzheimer's plaque protein Abeta has been shown to undergo reversible amyloid fibril formation to a position of dynamic equilibrium such that reaction thermodynamics can be quantified. Studies of these well-behaved amyloid systems are allowing us to peer more deeply into the process and products of off-pathway misfolding and aggregation.

Published 19 September 2006 in Acc Chem Res, 39(9): 671-9.
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