Supplementary Figure 6: Thermostability of amyloid fibrils formed by key segments of different amyloid proteins.
From: Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation
(a) FUS RAC1 and RAC2 segments form temperature-reversible amyloid fibrils. Mutation of RAC2 Y58F caused the formation of irreversible fibrils. Mutation of RAC2 Y58A prohibited the fibril assembly of RAC2. Some fibrils (thinner fibrils) formed by prion segment NNQQNY also dissolved as temperature increased. In contrast, pathogenic segments of Tau and Aβ formed highly thermal stable fibrils that are deemed to be closely related to AD. The scale bars are 200 nm. (b) Quantification of fibrils as temperature increases. The amount of fibrils was quantified by measuring the soluble peptide concentrations in the supernatant after ultracentrifugation (50,000 rpm for 50 min. Fibrils formed at 4 °C were ultracentrifuged at 4 °C; fibrils form at 20 °C and 50 °C were ultracentrifuged at 20 °C) at 205 nm using NANODROP 2000C (Thermo Scientific). Date shown are means and s.d. of n = 3 biologically independent samples.
