Abstract
Amyloid β19-20 peptide (Aβ19-20), a core recognition motif of the Alzheimer's β-amyloid fiber peptide, in vitro self-assembled into architectural wires is reported. Large quantities of well-ordered wires with diameters about 200nm spread out from nucleus. These wires have a high aspect ratio of at least 500 and a long persistence length over 100µm. We propose that formation of the hierarchical architectures is attributed to crystal-splitting mechanism. Effective π–π stacking between the aromatic residues and antiparallel β-sheet are predominant in the wires.
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