Solid-state NMR sequential assignment of an Amyloid-β(1–42) fibril polymorph

The formation of fibrils of the amyloid-β (Aβ) peptide is considered to be a key event in the pathology of Alzheimer’s disease (AD). The determination of a high-resolution structure of these fibrils is relevant for the understanding of the molecular basis of AD. In this work, we present the sequential resonance assignment of one of the polymorphs of Aβ(1–42) fibrils. We show that most of the protein is rigid, while a stretch of 4 residues (11–14) is not visible by solid-state NMR spectroscopy due to dynamics.