Fig. 1 Co-aggregation of Aβ16–22 and Aβ40 results in accelerated aggregation kinetics for Aβ40. Co-aggregation of Aβ16–22 and Aβ40 results in accelerated.

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Fig. 1 Co-aggregation of Aβ16–22 and Aβ40 results in accelerated aggregation kinetics for Aβ40. Co-aggregation of Aβ16–22 and Aβ40 results in accelerated aggregation kinetics for Aβ40. (A) Primary sequence of Aβ16–22 and Aβ40, including the groups at each terminus. The central recognition motif KLVFF is highlighted in purple. (B) ThT fluorescence assays showing that the aggregation rate of Aβ40 increases as the ratio of Aβ16–22 to Aβ40 is increased (with the total peptide concentration held constant at 40 μM). (C) Simulation snapshots of the aggregation of six Aβ40 monomers into a β-sheet–rich hexamer at an Aβ40 concentration of 5 mM. At the start of the simulation (0 μs), all the peptides are in random coils, but as the simulation progresses, they aggregate into antiparallel, in-register β sheets (104 μs). This oligomer then unfolds, losing some of its β-sheet structure (230 μs) before a rearrangement in which the β sheets rearrange, forming a stable fibril, with each Aβ40 peptide containing three β strands (621 μs) engaged in parallel intermolecular hydrogen bonding. 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).