title: Direct observation of amyloid fibril growth, propagation, and adaptation.
abstract: Amyloid fibrils form through nucleation and growth. To clarify the mechanism involved, direct observations of both processes are important. First, seed-dependent fibril growth of beta2-microglobulin (beta2-m) and amyloid beta peptide was visualized in real time at the single fibril level using total internal reflection fluorescence microscopy combined with the binding of thioflavin T, an amyloid-specific fluorescence dye. Second, using atomic force microscopy, ultrasonication-induced formation of beta2-m fibrils was shown, indicating that ultrasonication is useful to accelerate the nucleation process. Third, with the proteolytic fragment of beta2-m, propagation and a transformation of fibril morphology was demonstrated. These direct observations indicate that template-dependent growth and structural diversity are key factors determining the structure and function of amyloid fibrils.
authors.affiliation: Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.
authors.forename: Tadato
authors.initials: T
authors.lastname: Ban
authors.forename: Keiichi
authors.initials: K
authors.lastname: Yamaguchi
authors.forename: Yuji
authors.initials: Y
authors.lastname: Goto
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D008856:Microscopy, Fluorescence; D011487:Protein Conformation; D014465:Ultrasonics
chemical_list: D000682:Amyloid