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| Title | Amyloid-β nanotubes are associated with prion protein-dependent synaptotoxicity. |
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| Journal, issue, pages | Nat Commun, Vol. 4, Page 2416, Year 2013 |
| Publish date | Apr 1, 2014 |
 Authors | Andrew J Nicoll / Silvia Panico / Darragh B Freir / Daniel Wright / Cassandra Terry / Emmanuel Risse / Caroline E Herron / Tiernan O'Malley / Jonathan D F Wadsworth / Mark A Farrow / Dominic M Walsh / Helen R Saibil / John Collinge /  |
| PubMed Abstract | Growing evidence suggests water-soluble, non-fibrillar forms of amyloid-β protein (Aβ) have important roles in Alzheimer's disease with toxicities mimicked by synthetic Aβ(1-42). However, no ...Growing evidence suggests water-soluble, non-fibrillar forms of amyloid-β protein (Aβ) have important roles in Alzheimer's disease with toxicities mimicked by synthetic Aβ(1-42). However, no defined toxic structures acting via specific receptors have been identified and roles of proposed receptors, such as prion protein (PrP), remain controversial. Here we quantify binding to PrP of Aβ(1-42) after different durations of aggregation. We show PrP-binding and PrP-dependent inhibition of long-term potentiation (LTP) correlate with the presence of protofibrils. Globular oligomers bind less avidly to PrP and do not inhibit LTP, whereas fibrils inhibit LTP in a PrP-independent manner. That only certain transient Aβ assemblies cause PrP-dependent toxicity explains conflicting reports regarding the involvement of PrP in Aβ-induced impairments. We show that these protofibrils contain a defined nanotubular structure with a previously unidentified triple helical conformation. Blocking the formation of Aβ nanotubes or their interaction with PrP might have a role in treatment of Alzheimer's disease. |
 External links | Nat Commun / PubMed:24022506 / PubMed Central |
| Methods | EM (single particle) |
| Structure data |  EMDB-2433: |
| Source |
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Homo sapiens (human)