8OT3
unseeded Abeta(1-40) amyloid fibril (morphology ii)
Summary for 8OT3
| Entry DOI | 10.2210/pdb8ot3/pdb |
| EMDB information | 17167 |
| Descriptor | Amyloid-beta A4 protein (1 entity in total) |
| Functional Keywords | amyloid fibril, amyloid-beta, protein fibril |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 12 |
| Total formula weight | 52030.22 |
| Authors | |
| Primary citation | Pfeiffer, P.B.,Ugrina, M.,Schwierz, N.,Sigurdson, C.J.,Schmidt, M.,Fandrich, M. Cryo-EM Analysis of the Effect of Seeding with Brain-derived A beta Amyloid Fibrils. J.Mol.Biol., 436:168422-168422, 2023 Cited by PubMed Abstract: Aβ amyloid fibrils from Alzheimer's brain tissue are polymorphic and structurally different from typical in vitro formed Aβ fibrils. Here, we show that brain-derived (ex vivo) fibril structures can be proliferated by seeding in vitro. The proliferation reaction is only efficient for one of the three abundant ex vivo Aβ fibril morphologies, which consists of two peptide stacks, while the inefficiently proliferated fibril morphologies contain four or six peptide stacks. In addition to the seeded fibril structures, we find that de novo nucleated fibril structures can emerge in seeded samples if the seeding reaction is continued over multiple generations. These data imply a competition between de novo nucleation and seed extension and suggest further that seeding favours the outgrowth of fibril morphologies that contain fewer peptide stacks. PubMed: 38158175DOI: 10.1016/j.jmb.2023.168422 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.73 Å) |
Structure validation
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