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This hierarchical assembly provides a model, in which full-length Aβ transitions from an unfolded monomer to a folded β-hairpin, which assembles to form oligomers that further pack to form an annular pore.This model may provide a better understanding of the molecular basis of Alzheimer’s disease at atomic resolution.Two covalent constraints act in tandem to stabilize the Aβ17–36 peptide in a hairpin conformation: a δ-linked ornithine turn connecting positions 17 and 36 to create a macrocycle, and an intramolecular disulfide linkage between positions 24 and 29.
A detailed understanding of how materials structure on the nano- to meso-scale affects long-range charge transport behavior is needed to refine design rules for organic electronic devices.
β-Sheets are the building blocks of amyloid fibrils and oligomers.
Amyloid fibrils generally consist of extended networks of parallel β-sheets.