An amyloid-like fibril-forming supramolecular cross-β-structure of a model peptide: a crystallographic insight

Abstract

The peptideBoc-Val-Phe-OMe 1 bearing sequence similarity with the central hydrophobic cluster (CHC) of Alzheimer's Aβ^18-19peptide self-assembles to produce amyloid-like straight unbranched fibrils as examined by atomic force microscopy and Congo red assay. Single crystal X-ray diffraction offers the atomic level structure of the supramolecular parallel β-sheet aggregation and antiparallel separation between layers (cross-β-structure).