Article Title: The division of amyloid fibrils – Systematic comparison of fibril fragmentation stability by linking theory with experiments
Figure Lengend Snippet: Comparing the stability towards division of different amyloid fibril types. The decay of mean lengths (a), the division rate constants as function of fibril length (b), and the self-similar length distribution shapes (c) for hen egg Lyz (blue), bovine milk β-Lac (yellow), human α-Syn (red) and human β 2 m (black, data from Xue and Radford 2013 35 ) amyloid fibril samples undergoing division by fibril fragmentation under mechanical perturbation. All curves were calculated using α, γ, and g(x g ) obtained from our analysis of the experimental AFM images. In (a), the thicker portion of the lines denote the time range where the characteristic self-similar length distribution shape is observed in the imaging experiments (i.e. corresponding to the time regime represented by the solid fitted lines in Fig. 5 ), and crosses are the experimental data points that have closely reached the self-similar distribution shapes shown in the same plot. In (b), the thicker portion of the lines denote the range of fibril lengths observed experimentally on the AFM images. In (c), the distributions were calculated using self-similar distributions g(x g ) in Supplementary Fig. S3 after two weeks.
Article Snippet: 500 µ l aliquots were then heated without agitation for differing periods of time, with Lyz heated at 60 °C for 2 days and β-Lac heated at 90 °C for 5 hr. α-Syn fibrils were formed by buffer exchange of purified monomers into fibril forming buffer (20mM Sodium phosphate, pH7.5) using a PD-10 column (GE Healthcare).