Figure 8 | Scientific Reports

Figure 8

From: Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation

Figure 8

Isolation and biophysical characterization of helical intermediate.

(A) Schematic showing the isolation of helical intermediate. Secondary structure determined by CD spectroscopy for (B) helical mixture, (C) pellet, (D) supernatant, (E) retentate (isolated helix) and (F) flow through containing soluble α-Syn. (G) FTIR spectroscopy of isolated helix showing most intensity peak at 1653 cm−1 corresponding to helix conformation. (H) Morphological analysis for various isolated α-Syn species. AFM images are square of 5 micron and height scales are shown in individual AFM images.

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