title: Self-assembling nanomaterials: monitoring the formation of amyloid fibrils, with a focus on small-angle X-ray scattering.
abstract: Amyloid fibrils are attractive targets for applications in biotechnology. These thin, nanoscale protein fibers are highly ordered structures that self-assemble from their component proteins or peptides. This chapter describes the use of several biophysical techniques to monitor the formation of amyloid fibrils including a common dye-binding assay, turbidity assay, and small-angle X-ray scattering. These techniques provide information about the assembly mechanism, the rate and reproducibility of assembly, as well as the size of species along the assembly pathway.
authors.affiliation: Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Melbourne, Australia.
authors.forename: Elizabeth B
authors.initials: EB
authors.lastname: Sawyer
authors.forename: Sally L
authors.initials: SL
authors.lastname: Gras
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D000818:Animals; D052160:Benzothiazoles; D005456:Fluorescent Dyes / Q000737:chemistry; D006801:Humans; D009391:Nephelometry and Turbidimetry; D055503:Protein Multimerization; D053838:Scattering, Small Angle; D013050:Spectrometry, Fluorescence / Q000379:methods; D013844:Thiazoles / Q000737:chemistry; D014961:X-Ray Diffraction / Q000379:methods
chemical_list: D000682:Amyloid; D052160:Benzothiazoles; D005456:Fluorescent Dyes; D013844:Thiazoles; C009462:thioflavin T