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Kinetics and Thermodynamics of Amyloid Fibril Assembly

2006; American Chemical Society; Volume: 39; Issue: 9 Linguagem: Inglês

10.1021/ar050069h

1520-4898

Ronald Wetzel,

Protein Structure and Dynamics

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 Aβ 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.