Solid-state NMR as a probe of amyloid fibril structure

Amyloid fibrils are intrinsically noncrystalline, insoluble, high-molecular -weight aggregates of peptides and proteins, with considerable biomedical a nd biophysical significance. Solid-state NMR techniques are uniquely capabl e of providing high-resolution, site-specific structural constraints for am yloid fibrils, at the level of specific interatomic distances and torsion a ngles. So far, a relatively small number of solid-state NMR studies of amyl oid fibrils have been reported. These have addressed issues about the supra molecular organization of beta-sheets in the fibrils and the peptide confor mation in the fibrils, and have concentrated on the beta-amyloid peptide of Alzheimer's disease. Many additional applications of solid-state NMR to am yloid fibrils from a variety of sources are anticipated in the near future, as these systems are ideally suited for the technique and are of widesprea d current interest.