Structural Insight into an Alzheimer’s Brain-Derived Spherical Assembly of Amyloid β by Solid-State NMR
作者： Sudhakar Parthasarathy , Masafumi Inoue , Yiling Xiao , Yoshitaka Matsumura , Yo-ichi Nabeshima
DOI: 10.1021/JACS.5B03373
关键词: Solid-state nuclear magnetic resonance 、 Amyloid β 、 Protein folding 、 Biochemistry 、 Conformational isomerism 、 Amyloid disease 、 Chemistry 、 Alzheimer's disease 、 Neurotoxin 、 Amyloid
摘要: Accumulating evidence suggests that various neurodegenerative diseases, including Alzheimer's disease (AD), are linked to cytotoxic diffusible aggregates of amyloid proteins, which metastable intermediate species in protein misfolding. This study presents the first site-specific structural on an called amylospheroid (ASPD), AD-derived neurotoxin composed oligomeric amyloid-β (Aβ). Electron microscopy and immunological analyses using ASPD-specific "conformational" antibodies established synthetic ASPD for 42-residue Aβ(1-42) as excellent structural/morphological analogue native extracted from AD patients, level correlates with severity AD. (13)C solid-state NMR approximately 20 residues interstrand distances demonstrated is made a homogeneous single conformer containing parallel β-sheets. These results provide profound insight into ASPD, indicating Aβ likely self-assemble toxic β-sheet structures brains. approach can be applied intermediates relevant diseases.
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