Recent results from structural studies of amyloid fibrils formed by the 40-residue Aβ peptide and by the low-complexity domain of the FUS protein (and portions thereof) will be presented. These structural studies use both solid state NMR and cryoEM methods. In the case of Aβ fibrils, we have found a surprising two-fold symmetric polymorph with a mass-per-length value of 27 kDa/nm (indicating three peptide molecules per β-sheet repeat spacing). In the case of FUS fibrils, we have found that two different, non-overlapping segments of the 214-residue low-complexity domain can form a structurally ordered fibril core, although only one of these is populated when the full-length sequence self-assembles.

Structure of amyloid-β and FUS low-complexity domain fibrils

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.