Direct observation of amyloid fibril growth, propagation, and adaptation.
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.
Ban
Tadato
T
Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.
Yamaguchi
Keiichi
K
Goto
Yuji
Y
D000682:Amyloid / Q000737:chemistry*; D008856:Microscopy, Fluorescence; D011487:Protein Conformation; D014465:Ultrasonics
D000682:Amyloid