Interaction between soluble Aβ-(1-40) monomer and Aβ-(1-42) fibrils probed by paramagnetic relaxation enhancement.

• Yamaguchi, Takahiro

• Matsuzaki, Katsumi

• 星野, 大

抄録

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).

収録刊行物

• FEBS letters

  FEBS letters 587 (6), 620-624, 2013-03-18

  Elsevier BV

キーワード

• Nuclear magnetic resonance
• Paramagnetic relaxation enhancement
• Cross seeding
• Amyloid fibril
• Dock-Lock model

詳細情報

• CRID: 1050845760697434240
• NII論文ID: 120005244251
• NII書誌ID: AA00642943
• ISSN: 00145793
• ISSN: 18733468
• HANDLE: 2433/173120
• 本文言語コード: en
• 資料種別: journal article
• データソース種別:
  • IRDB
  • CiNii Articles