CHAPTER 28: Solid-State NMR Studies of β-Amyloid Fibrils and Related Assemblies
Published:24 Feb 2014
W. Qiang and R. Tycko, in Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides, ed. F. Separovic and A. Naito, The Royal Society of Chemistry, 2014, pp. 556-576.
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The β-amyloid (Aβ) peptide forms a variety of fibrillar and non-fibrillar assemblies in human brain tissue, especially in Alzheimer's disease (AD). Over the past 20 years, solid-state NMR methods have played a major role in the elucidation of the molecular structures of Aβ assemblies. This chapter reviews progress in this research area, including structural studies of fibrils formed by Aβ fragments, full-length Aβ peptides, and disease-associated mutants, as well as studies of Aβ oligomers and protofibrils, Aβ/membrane interactions, and interactions of Aβ with metal ions.