Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 133, Issue 40, Pages 16013-16022Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja2035859
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Funding
- WeNMR project (European FP7 e-Infrastructure grant) [261572]
- Bio-NMR project (European FP7 e-Infrastructure grant) [261863]
- INSTRUCT (European FP7 e-Infrastructure grant) [211252]
- Ente Cassa Risparmio Firenze
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The amyloid fibrils of beta-amyloid (A beta) peptides play important roles in the pathology of Alzheimer's disease. Comprehensive solid-state NMR (SSNMR) structural studies on uniformly isotope-labeled A beta 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 A beta(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-beta-strand contacts within the U-shaped beta-strand-turn-beta-strand motif are shifted, the N-terminal region adopts a beta-conformation, and new inter-monomer contacts occur at the protofilament interface. The revealed structural diversity in A beta fibrils points to a complex picture of A beta fibrillation.
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