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Open Access Green as soon as Postprint is submitted to ZB.
Structural properties of EGCG-induced, nontoxic Alzheimer's disease Aβ oligomers.
J. Mol. Biol. 421, 517-524 (2012)
The green tea compound epigallocatechin-3-gallate (EGCG) inhibits Alzheimer's disease beta-amyloid peptide (A beta) neurotoxicity. Solution-state NMR allows probing initial EGCG-A beta interactions. We show that EGCG-induced A beta oligomers adopt a well-defined structure and are amenable for magic angle spinning solid-state NMR investigations. We find that EGCG interferes with the aromatic hydrophobic core of A beta. The C-terminal part of the A beta peptide (residues 22-39) adopts a beta-sheet conformation, whereas the N-terminus (residues 1-20) is unstructured. The characteristic salt bridge involving residues D23 and K28 is present in the structure of these oligomeric A beta aggregates as well. The structural analysis of small-molecule-induced amyloid aggregates will open new perspectives for Alzheimer's disease drug development.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Alzheimer's Disease ; Beta-amyloid Peptide ; Magic Angle Spinning (mas) Solid-state Nmr Spectroscopy ; Drug Development ; Neurotoxicity; Solid-State Nmr; Amyloid Fibrils; Green Tea; Experimental Constraints; Peptide; Toxicity; Inhibitors; (-)-Epigallocatechin-3-Gallate; Neurotoxicity; Spectroscopy
ISSN (print) / ISBN
0022-2836
e-ISSN
1089-8638
Journal
Journal of Molecular Biology
Quellenangaben
Volume: 421,
Issue: 4-5,
Pages: 517-524
Publisher
Elsevier
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)