|Title:||Interaction between soluble Aβ-(1-40) monomer and Aβ-(1-42) fibrils probed by paramagnetic relaxation enhancement.|
Matsuzaki, Katsumi https://orcid.org/0000-0002-0182-1690 (unconfirmed)
Hoshino, Masaru https://orcid.org/0000-0003-4099-0232 (unconfirmed)
|Author's alias:||星野, 大|
|Keywords:||Nuclear magnetic resonance|
Paramagnetic relaxation enhancement
|Journal title:||FEBS letters|
|Abstract:||The most common isoforms of amyloid-β (Aβ) proteins are composed of 40 or 42 amino acid residues. While Aβ-(1-40) is the predominant species, Aβ-(1-42) is more fibrillogenic and neurotoxic, suggesting that Aβ-(1-42) plays a critical role in the initiation of amyloid fibril formation. We investigated the mechanisms by which soluble Aβ-(1-40) associates with preformed Aβ-(1-42) seeds. A paramagnetic relaxation enhancement analysis showed that the Aβ-(1-40) monomer and Aβ-(1-42) seed interact via their C-terminal region in a parallel fashion, and the N-terminal part does not to contribute to the interaction. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: A beta-(1-40) and A beta-(1-42)bind by fluorescence technology (View interaction) A beta-(1-42) and A beta-(1-40)bind by nuclear magnetic resonance (View interaction).|
|Rights:||© 2013 Federation of European Biochemical Societies. Published by Elsevier B.V.|
This is not the published version. Please cite only the published version.
|Appears in Collections:||Journal Articles|
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