Fig. 2: Characterization of N21Q cytotoxic fibrils. | Communications Biology

Fig. 2: Characterization of N21Q cytotoxic fibrils.

From: Identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies

Fig. 2

a, b Representative images of flat and twisted IAPP and N21Q fibrils revealed by a TEM and b AFM. Scale bar: 100 nm. c Distributions of mesoscopic morphology and stiffness of over 3000 fibrils per peptide imaged by AFM. d ATR-FTIR absorbance spectra of the amide I region (1500–1800 cm−1) of IAPP and N21Q fibrils. e Far-UV circular dichroism spectra of IAPP and N21Q fibrils. f ThT fluorescence of fibrils. Emission spectra of ThT (40 μM) with an excitation at 440 nm. g Surface hydrophobicity measured by ANS fluorescence. Emission spectra of ANS (100 μM) with an excitation at 355 nm. h Powder XRD diffraction spectra revealing a periodic amyloid packing for IAPP and N21Q fibrils. a–h Fibrils were assembled from freshly dissolved monomerized peptides incubated under quiescent conditions for 48 h at 150 µM in 20 mM Tris–HCl buffer, pH 7.4. Assemblies were diluted to 10 μM (a–c) and 50 μM (e–g), immediately before analysis.

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