Solid-State NMR Spectroscopic Investigation of Aβ Protofibrils: Implication of a β-Sheet Remodeling upon Maturation into Terminal Amyloid Fibrils

The secondary structure elements in Aβ protofibrils (see TEM image) were determined at a single residue level by solid‐state NMR spectroscopy. The β‐sheet elements of the mature fibrils are already preformed in protofibrils, but these regions have to elongate during the conversion into mature fibril...

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Bibliographic Details
Published in:Angewandte Chemie (International ed.) 2011-03, Vol.50 (12), p.2837-2840
Main Authors: Scheidt, Holger A, Morgado, Isabel, Rothemund, Sven, Huster, Daniel, Fändrich, Marcus
Format: Article
Language:English
Subjects:
Alzheimer
Alzheimer Disease - metabolism
Amyloid - chemistry
amyloid beta-peptide
Amyloid beta-Peptides - chemistry
Amyloid beta-Peptides - ultrastructure
fibrous proteins
Humans
Magnetic Resonance Spectroscopy
NMR spectroscopy
Peptide Fragments - chemistry
Peptide Fragments - ultrastructure
Protein Structure, Secondary
protofibrils
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Summary:The secondary structure elements in Aβ protofibrils (see TEM image) were determined at a single residue level by solid‐state NMR spectroscopy. The β‐sheet elements of the mature fibrils are already preformed in protofibrils, but these regions have to elongate during the conversion into mature fibrils. The data have important implications for understanding the process of fibril formation in general as well as the structural basis of Alzheimer's disease.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201007265