Figure 1
Synucleins fibrillation through helix-rich intermediate.
(A) Aggregation of synucleins was monitored by ThT fluorescence. All synucleins (LMW) were incubated at 37°C with slight agitation at a concentration of 300 μM in 20 mM Gly-NaOH buffer, 0.01% sodium azide, pH 7.4. ThT fluorescence was performed at regular intervals. ThT fluorescence intensities at 480 nm were ploted against incubation time for each protein. (B) Bar diagram representation of lag time for the synucleins aggregation kinetics monitored by ThT fluorescence. (C) CD spectroscopy reveals synucleins were initially random coil and converted to β-sheet conformation via α-helix-rich intermediate. The different colored numbers indicate the incubation times (hrs). Selected CD spectra were shown.
