Structure of the cross-β spine of amyloid-like fibrils

By R. Nelson, M. Sawaya, M. Balbirnie, A. Madsen, C. Riekel, R. Grothe, David S. Eisenberg. Nature, 2005

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Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. (2006, background): “As represented in recent models for amyloid structures (7, 10, 14, 29, 36, 42, 44, 51-59) and supported by recent x-ray crystal structures of short amyloid-forming peptides ( 60 ), the core of an amyloid fibril contains two or more layers of β-sheets.”
Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils (2008, background): “In addition to creating a hydrophobic core, the parallel nature of the -sheets may permit ‘‘polar zipper’’ interactions among Q15 sidechains (31), which fit into a cavity created by G37 and G38 in a manner reminiscent of the ‘‘steric zippers’’ that have been observed in amyloid-like peptide crystal ”
Functional amyloid--from bacteria to humans. (2007, background): “and microcrystal-based [ 73 ] high-resolution structures of peptidederived amyloid fibers, revealing an all-parallel b-sheet quaternary”