A new structural model of Aβ 40 fibrils
| Autor: | Claudio Luchinat, Antonella Nesi, Leonardo Gonnelli, Jiafei Mao, Ivano Bertini |
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| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular 0303 health sciences Amyloid Amyloid beta-Peptides Chemistry Structural diversity General Chemistry 010402 general chemistry Fibril Amyloid fibril 01 natural sciences Biochemistry Catalysis Peptide Fragments Protein Structure Secondary 3. Good health 0104 chemical sciences 03 medical and health sciences Crystallography Colloid and Surface Chemistry Protein structure Alzheimer Disease Humans Nuclear Magnetic Resonance Biomolecular 030304 developmental biology |
| Zdroj: | Journal of the American Chemical Society |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/ja2035859 |
| Popis: | The amyloid fibrils of beta-amyloid (Aβ) peptides play important roles in the pathology of Alzheimer's disease. Comprehensive solid-state NMR (SSNMR) structural studies on uniformly isotope-labeled Aβ assemblies have been hampered for a long time by sample heterogeneity and low spectral resolution. In this work, SSNMR studies on well-ordered fibril samples of Aβ(40) with an additional N-terminal methionine provide high-resolution spectra which lead to an accurate structural model. The fibrils studied here carry distinct structural features compared to previous reports. The inter-β-strand contacts within the U-shaped β-strand-turn-β-strand motif are shifted, the N-terminal region adopts a β-conformation, and new inter-monomer contacts occur at the protofilament interface. The revealed structural diversity in Aβ fibrils points to a complex picture of Aβ fibrillation. |
| Databáze: | OpenAIRE |
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