title: Interaction between soluble Aβ-(1-40) monomer and Aβ-(1-42) fibrils probed by paramagnetic relaxation enhancement.
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.
authors: Graduate School of Pharmaceutical Sciences, Kyoto University, 46-29 Yoshida-Shimoadachi, Sakyo-ku, Kyoto 606-8501, Japan.
authors: Takahiro
authors: T
authors: Yamaguchi
authors: Katsumi
authors: K
authors: Matsuzaki
authors: Masaru
authors: M
authors: Hoshino
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry*; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D010446:Peptide Fragments / Q000737:chemistry*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry; D012995:Solubility; D012996:Solutions; D013113:Spin Labels
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; D011994:Recombinant Proteins; D012996:Solutions; D013113:Spin Labels; C078592:amyloid beta-protein (1-40); C075222:amyloid beta-protein (1-42)