Figure 1: Aβ40-DI CAA mutant amyloid fibril seeds promote the rapid assembly of wild-type Aβ40 and Aβ42 fibrils. | Nature Communications

Figure 1: Aβ40-DI CAA mutant amyloid fibril seeds promote the rapid assembly of wild-type Aβ40 and Aβ42 fibrils.

From: Cerebral vascular amyloid seeds drive amyloid β-protein fibril assembly with a distinct anti-parallel structure

Figure 1

(a) FTIR spectra of Aβ40-DI having anti-parallel (green) and parallel (black) β-sheet secondary structure. The anti-parallel fibrils were formed at 4-6 °C using the protocol of Tycko22,23 (Supplementary Fig. 2) and are stable to at least 22 °C (Supplementary Fig. 3). (b) TEM of anti-parallel Aβ40-DI obtained at 22 °C. Scale bar, 150 nm. Freshly prepared solutions of wild-type Aβ40 (c,d) or wild-type Aβ42 (e,f) were incubated in the absence (blue) or presence (red) of parallel (c,e) or anti-parallel (d,f) Aβ40-DI fibrillar seeds. The rate and extent of fibril formation was assessed by thioflavin T fluorescence measurements at 37 °C. TEM, transmission electron microscopy.

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