Fig. 5: Structural changes of α-Synuclein fibrils in the presence of compounds. | npj Parkinson's Disease

Fig. 5: Structural changes of α-Synuclein fibrils in the presence of compounds.

From: An approach to characterize mechanisms of action of anti-amyloidogenic compounds in vitro and in situ

Fig. 5

A Fingerprint of EGCG treated α-Synuclein fibril compared to untreated α-Synuclein fibril (upper panel control peptide analysis, middle panel amino acid analysis of LiP results, lower panel predicted interaction sites). The position of lysine residues is shown. The scale indicates the score per amino acid. The significance threshold of −log10(0.05) × log2(2) is shown in white, with red indicating higher scores. The more intense the red color, the higher the score. Not significant in gray. Not detected in pale yellow. B EGCG fingerprint mapped on the α-Synuclein fibril structure (pdb: 6cu7); color scheme as in (A). C–H Fingerprints of the comparison of the untreated α-Synuclein fibril structure and α-Synuclein fibrils treated with Baicalein (C), Doxycycline (D), Thioflavin T (E), compound 2 (F), compound 1 (G) and Fasudil (H). Scales in panels C–H are indicated, colors are as in (A).

Back to article page