Fig. 3: Fluorescent dyes distinguish aSyn aggregate structures.
From: Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts
a–c Normalized fluorescence spectra of curcumin (a), HS-68 (b) and FSB (c) in the presence of amyloid fibrils amplified from brain extracts of different patients (Table 1; PD/green, MSA/purple), as well as two in vitro aSyn polymorphs (hsAsyn/blue, lsAsyn/red)5,6. d, e PCA of fluorescence spectra of the amyloid-binding dyes curcumin and HS-68 (d), and curcumin and FSB (e), in presence of aSyn fibrils. aSyn fibrils amplified from patient brain-extracts are identified according to Table 1. In addition to brain-extract amplified fibrils, the fluorescence spectra of various in vitro polymorphs were analyzed: hsAsyn (blue), lsAsyn (red), and amyloid fibrils formed through de novo aggregation under conditions of PMCA (termed de novo PMCA; yellow). For each sample, fluorescence spectra of the three dyes were measured independently twice, and the resulting values were joined combinatorially resulting in four data points per sample in order to represent the intrinsic variability in the fluorescence measurements.
