Figure 9
‘On pathway’ α-helical intermediate during synuclein fibrilization.
(A) CD spectra during aggregation showing conversion from isolated helix-rich state to β-sheet upon incubation. (B) Kinetics of aggregation of LMW α-Syn and isolated helix monitored by ThT. (C) Morphological analysis of fibrils formed from isolated helix (left panel) and LMW α-Syn (right panel) by AFM. Scale bar are 500 nm. Height scales (upper panel) and amplitude scales (lower panel) are shown in individual AFM images. (D) Morphological characterization of the fibrils formed by the isolated helix in presence of externally added fibrils by AFM showing regular characteristic of thin and long fibrils morphology. Scale bar are 500 nm. Height scales (left panel) and amplitude scales (right panel) are shown in individual AFM images. (E) Seeding capacity of isolated helical intermediate and fibrils. The presence of 10% (v/v) helical intermediate and fibrils in a sample containing 300 μM LMW α-Syn reduced the lag phase of α-Syn fibril formation. α-Syn without any seeds was used as a control.
