Fig. 3
Schematic figure of the hypothesis of distinguishing amyloid fibril structures by amyloid dyes. (1) Two different amyloid fibril structures both contain the Congo red amyloid binding site (illustrated by PyMol of PDB 2LBU from33). (2) Co-staining with the rigid X-34 (blue fluorescent) and the flexible (HS-310) amyloid dye demonstrated by free rotations between the thiophene rings. Both ligands preferably binds to the Congo red binding site on the fibril. (3) Shape of the binding site determines preference. (4) The readout of the analysis is performed by the spectral output of the stained tissue amyloid deposits with hyperspectral microscopy by the comparative intensity of the 471 nm emission peak for X-34 (blue) and 552 nm peak for HS-310 (orange). The arrows indicate the spectral output for the respective fibril binding site preference.
