Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer's β-Amyloid Peptide, and Structural Characterization by Solid State NMR†

By J. Balbach, Y. Ishii, O. Antzutkin, Richard Leapman, N. Rizzo, F. Dyda, J. Reed, R. Tycko. 2000

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Supramolecular Structure in Full-Length Alzheimer's β-Amyloid Fibrils: Evidence for a Parallel β-Sheet Organization from Solid-State Nuclear Magnetic Resonance (2002, background): “The experimental observation of an in-register parallel -sheet organization in amyloid fibrils formed by peptides with asymmetrically distributed hydrophobic segments, such as A 1–40, A 10–35, and A 1–42, suggests that intermolecular hydrophobic interactions play a dominant role in determining the s”
Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. (2006, background): “the primary stabilizing interactions in Aβ1-40 fibrils and in fibrils formed by certain other peptides (8, 10, 37, 41), may account for the polymorphism of Aβ1-40 fibrils.”