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. Author manuscript; available in PMC: 2016 Dec 11.
Published in final edited form as: J Am Chem Soc. 2016 Jul 28;138(31):9840–9852. doi: 10.1021/jacs.6b03715

Figure 1.

Figure 1

Fibrillization of wild-type, Arctic and Osaka Aβ40 peptides. (A) Osaka and Arctic Aβ40 peptides form fibrils much more rapidly than the wild-type (WT) peptide. Kinetics of fibril formation (0.2 mg/ml in 10 mM sodium phosphate buffer, pH 7.2) was measured by the amyloid-binding dye ThT (10 μM). n=5, mean±SEM. (B) Negative stain TEM images of WT and mutant Aβ40 fibrils. Arctic Aβ40 fibrils display significant twists with variable periodicities and more pronounced entanglement than wild-type and Osaka fibrils. Scale bar = 100 nm. (C) Mutant fibrils have altered stability to denaturation by GdnHCl. Fibrils were incubated with increasing concentrations (1 – 6 M) of GdnHCl and then ultracentrifuged at 100,000 × g to pellet any fibrils that resisted denaturation, which were resolved by SDS-PAGE and Coomassie stain.