title: Diagnostics for amyloid fibril formation: where to begin?
abstract: Twenty-five proteins are known to form amyloid fibrils in vivo in association with disease (Westermark et al., Amyloid 12:1-4, 2005). However, the fundamental ability of a protein to form amyloid-like fibrils is far more widespread than in just the proteins associated with disease, and indeed this property can provide insight into the basic thermodynamics of folding and misfolding pathways. But how does one determine whether a protein has formed amyloid-like fibrils? In this chapter, we cover the basic steps toward defining the amyloid-like properties of a protein and how to measure the kinetics of fibrillization. We describe several basic tests for aggregation and the binding to two classic amyloid-reactive dyes, Congo Red, and thioflavin T, which are key indicators to the presence of fibrils.
authors.affiliation: Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC, Australia. dhatters@unimelb.edu.au
authors.forename: Danny M
authors.initials: DM
authors.lastname: Hatters
authors.forename: Michael D W
authors.initials: MD
authors.lastname: Griffin
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D052160:Benzothiazoles; D001718:Birefringence; D002498:Centrifugation; D002850:Chromatography, Gel; D003224:Congo Red / Q000737:chemistry; D007700:Kinetics; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D013057:Spectrum Analysis / Q000379:methods*; D013844:Thiazoles / Q000737:chemistry
chemical_list: D000682:Amyloid; D052160:Benzothiazoles; D013844:Thiazoles; C009462:thioflavin T; D003224:Congo Red