Fig. 4 Aβ16–22 fibrils increase the aggregation rate of Aβ40 to a greater extent than Aβ16–22 monomers. Aβ16–22 fibrils increase the aggregation rate of.

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Fig. 4 Aβ16–22 fibrils increase the aggregation rate of Aβ40 to a greater extent than Aβ16–22 monomers. Aβ16–22 fibrils increase the aggregation rate of Aβ40 to a greater extent than Aβ16–22 monomers. (A) Increased concentrations (% w/w) of Aβ16–22 fibrils were added to Aβ40 monomers (as shown in the key), and the aggregation rate was measured by ThT fluorescence. (B) Direct comparison of the effect of Aβ16–22 monomers (i.e., taken straight from a DMSO stock) and Aβ16–22 fibrils on Aβ40 aggregation. (C) Effect of sonicating the Aβ16–22 fibrils on the Aβ40 aggregation rate shows little effect compared with the data shown in (A) (see text for details). (D) Plots of the percent β sheet formed by Aβ40 in the absence (blue) or presence of preformed two (black), three (red), or four (green) β-sheet Aβ16–22, determined using DMD, showing that an increased Aβ16–22 fibril size increases the rate of Aβ40 aggregation. (E) During co-aggregation experiments, both elongation and surface-catalyzed mechanisms can occur; each has a different effect on the rate of assembly of each peptide (the same notation is used as in Fig. 3E, with circles representing monomers, blocks representing fibrils, and Aβ16–22 and Aβ40 in red and blue, respectively). Adapted from (24). Samuel J. Bunce et al. Sci Adv 2019;5:eaav8216 Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY).