Fig. 4: Structural changes within monomeric α-Synuclein in the presence of compounds. | npj Parkinson's Disease

Fig. 4: Structural changes within monomeric α-Synuclein in the presence of compounds.

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

Fig. 4

A Fingerprint of EGCG-treated α-Synuclein monomer compared to untreated α-Synuclein monomer. The upper panel indicates control (trypsin-only) peptide analysis. The lower panel indicates amino acid-level analysis of LiP peptides; the scales in both fingerprints (i.e., black to red) indicates the score per amino acid or peptide. 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 and black. Not detected in pale yellow. B NMR spectra of α-Synuclein with 10 x EGCG. C MTSL/no MTSL of no EGCG (light gray) and 10 x EGCG (red) treated α-Synuclein monomer. D ThT assay with ΔN (Δ2-11) - and ΔC (Δ122-140) α-Synuclein treated with 10 x EGCG. E–J Fingerprints of the comparison of the untreated α-Synuclein monomer structure and α-Synuclein monomers treated with Baicalein (E), Doxycycline (F), compound 2 (G), compound 1 (H), Thioflavin T (I) and Fasudil (J). Scales in panels E–J are indicated, colors are as in (A).

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