Structure of Amyloid fibris

Amyloid fibrils, filamentous aggregates of proteins or peptides, have been known to be related to causes of number of neuronal diseases. Understanding of how monomer units are structured and arranged each other in the fibrils is crucial to elucidate the physical basis of its formation and deposition. Answering this question is important for obtaining further insight into the mechanism of protein folding and misfolding in general.

Recently, it has been found that amyloid fibrils are amenable to the most sophisticated magic-angle-spinning (MAS) solid-state NMR methods, providing structural information at atomic resolution that otherwise has been inaccessible.

Recently, We have combined solid-state NMR, x-ray fiber diffraction, and atomic force microscopy to reveal the 3D structure of amyloid protofilament-like fibrils formed by a 22-residue K3 peptide (Ser20-Lys41) of beta2-microglobulin, a protein responsible for dialysis-related amyloidosis. By revealing the structure of beta2-microglobulin protofilament-like fibrils, this work represents technical progress in analyzing amyloid fibrils in general through solid-state NMR. (Publication, Iwata et al. PNAS (2006))