Interaction between soluble Aβ‐(1–40) monomer and Aβ‐(1–42) fibrils probed by paramagnetic relaxation enhancement. Issue 6 (15th February 2013)

• Record Type: Journal Article
• Authors: Yamaguchi, Takahiro; Matsuzaki, Katsumi; Hoshino, Masaru
• Is Part Of: FEBS letters. Volume 587:Issue 6(2013)
• Page Start: 620
• Page End: 624
• Publication Date: 2013-02-15
• Subjects: AD -- Alzheimer's disease -- Aβ -- amyloid-β peptide -- HSQC -- heteronuclear single-quantum coherence -- MTSL -- (1-oxyl-2, 2, 5, 5-tetramethyl-Δ3-pyrroline-3-methyl) methanethiosulfonate -- NMR -- nuclear magnetic resonance -- PRE -- paramagnetic relaxation enhancement -- Nuclear magnetic resonance -- Paramagnetic relaxation enhancement -- Cross seeding -- Amyloid fibril -- Dock-Lock model; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.02.008
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : A beta‐(1–42) and A beta‐(1–40) bind by nuclear magnetic resonance (View interaction) Abstract : ► The growth of Aβ‐(1–40) fibrils from Aβ‐(1–42) seeds exhibited a lag phase. ► The Aβ‐(1–40) monomer and Aβ‐(1–42) seed interacted via their C‐terminal region. ► The N‐terminal part of the molecule did not contributed to the interaction.