Fiber Diffraction Data Indicate a Hollow Core for the Alzheimerʹs Aβ 3-Fold Symmetric Fibril

Amyloid β protein (Aβ), the principal component of the extracellular plaques found in the brains of patients with Alzheimerʹs disease, forms fibrils well suited to structural study by X-ray fiber diffraction. Fiber diffraction patterns from the 40-residue form Aβ(1–40) confirm a number of features of a 3-fold symmetric Aβ model from solid‐state NMR (ssNMR) but suggest that the fibrils have a hollow core not present in the original ssNMR models. Diffraction patterns calculated from a revised 3-fold hollow model with a more regular β-sheet structure are in much better agreement with the observed diffraction data than patterns calculated from the original ssNMR model. Refinement of a hollow-core model against ssNMR data led to a revised ssNMR model, similar to the fiber diffraction model.