13 C and 15 N chemical shift assignments of mammalian Y145Stop prion protein amyloid fibrils

Biomol NMR Assign. 2017 Apr;11(1):75-80. doi: 10.1007/s12104-016-9723-6. Epub 2016 Dec 21.

Abstract

The Y145Stop prion protein (PrP23-144), which has been linked to the development of a heritable prionopathy in humans, is a valuable in vitro model for elucidating the structural and molecular basis of amyloid seeding specificities. Here we report the sequential backbone and side-chain 13C and 15N assignments of mouse and Syrian hamster PrP23-144 amyloid fibrils determined by using 2D and 3D magic-angle spinning solid-state NMR. The assigned chemical shifts were used to predict the secondary structures for the core regions of the mouse and Syrian hamster PrP23-144 amyloids, and the results compared to those for human PrP23-144 amyloid, which has previously been analyzed by solid-state NMR techniques.

Keywords: Amyloid; Magic-angle spinning; Prion protein; Solid-state NMR.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Amyloid / chemistry*
  • Animals
  • Cricetinae
  • Mice
  • Nuclear Magnetic Resonance, Biomolecular*
  • Peptide Fragments / chemistry
  • Prion Proteins / chemistry*
  • Protein Multimerization*
  • Protein Structure, Secondary

Substances

  • Amyloid
  • Peptide Fragments
  • Prion Proteins