title: Kinetics and thermodynamics of amyloid fibril assembly.
abstract: 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.
authors.affiliation: Graduate School of Medicine, University of Tennessee, 1924 Alcoa Highway, Knoxville, Tennessee 37920, USA.
authors.forename: Ronald
authors.initials: R
authors.lastname: Wetzel
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D007700:Kinetics; D013816:Thermodynamics
chemical_list: D000682:Amyloid