Fig. 3 Aβ16–22 can interact with Aβ40 monomers and dimers.

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Presentation transcript:

Fig. 3 Aβ16–22 can interact with Aβ40 monomers and dimers. Aβ16–22 can interact with Aβ40 monomers and dimers. (A) Native ESI-IMS-MS drift-scope images of Aβ40 indicate the presence of multiple oligomeric species of Aβ40 (white numbers). (B) When mixed at a 1:1 mol/mol ratio with Aβ16–22 (yellow numbers), a number of heteromeric species are observed (light blue numbers) immediately following mixing. The oligomer size is given (1, 2, 3, etc.), with the charge state in superscript. (C) DMD simulation showing the percent β sheet formed by Aβ40 during aggregation in the absence (black) or presence (red) of Aβ16–22. (D) Energy contact map between one monomer of Aβ16–22 and one of Aβ40 scaled by energy (bar shown alongside), showing that residues 17 to 20 (LVFF) and 31 to 34 (IIGL) form the strongest interactions. (E) Co-aggregation can have differing effects on the primary nucleation of each peptide, depending on whether the mixed oligomers formed can progress to form mixed fibrils or are off-pathway and take no further part in the aggregation reaction. Circles represent monomers and blocks represent fibrils, with 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).