The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy.

ABSTRACT: Structural analysis of protein fibrillation is inherently challenging. Given the crucial role of fibrils in amyloid diseases, method advancement is urgently needed. A hybrid modelling approach is presented enabling detailed analysis of a highly ordered and hierarchically organized fibril of the GNNQQNY peptide fragment of a yeast prion protein. Data from small-angle X-ray solution scattering, fibre diffraction and electron microscopy are combined with existing high-resolution X-ray crystallographic structures to investigate the fibrillation process and the hierarchical fibril structure of the peptide fragment. The elongation of these fibrils proceeds without the accumulation of any detectable amount of intermediate oligomeric species, as is otherwise reported for, for example, glucagon, in

SUBMITTER: Langkilde AE 

PROVIDER: S-EPMC4388266 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature