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. 2016 Apr 13;7:11359. doi: 10.1038/ncomms11359

Figure 1. Aβ aggregates have distinct pressure stability.

Figure 1

(a) Electron micrographs of aggregated Aβ40 in its non-phosphorylated (npAβ) and S8-phosphorylated (pS8Aβ) state reveal amyloid fibrils of similar morphology. Scale bar, 500 nm. (b) Pressure dependence of Aβ monomer release from npAβ (magenta) and pS8Aβ (green) aggregates. Error bars represent the s.d. between three consecutive measurements each taking 10 min. (c) Time dependence of Aβ monomer release, as followed by NMR signal intensities, on incubation of aggregated Aβ at a hydrostatic pressure of 2,000 bar. Data fit to mono- and bi-exponential functions are presented in dotted and solid lines, respectively. Phosphorylation at S8 attenuates the monomer release from Aβ40 aggregates. In addition, Aβ42 aggregates (red) are more stable than Aβ40 aggregates.