Structure of amyloid-β (20-34) with Alzheimer’s-associated isomerization at Asp23 reveals a distinct protofilament interface
oleh: Rebeccah A. Warmack, David R. Boyer, Chih-Te Zee, Logan S. Richards, Michael R. Sawaya, Duilio Cascio, Tamir Gonen, David S. Eisenberg, Steven G. Clarke
| Format: | Article |
|---|---|
| Diterbitkan: | Nature Portfolio 2019-07-01 |
Deskripsi
In patients with sporadic Alzheimer’s disease part of the Asp23 residues are isomerized to L-isoaspartate (L-isoAsp23). Here the authors present the MicroED structures of wild-type and L-isoAsp23 Aβ 20–34 amyloid fibrils that both form tightly packed cores and self-associate through two distinct interfaces with one of these interfaces being strengthened by the isoaspartyl modification.