Solid-state NMR sequential assignment of an Amyloid-β(1-42) fibril polymorph

Biomol NMR Assign. 2016 Oct;10(2):269-76. doi: 10.1007/s12104-016-9682-y. Epub 2016 May 10.

Abstract

The formation of fibrils of the amyloid-β (Aβ) peptide is considered to be a key event in the pathology of Alzheimer's disease (AD). The determination of a high-resolution structure of these fibrils is relevant for the understanding of the molecular basis of AD. In this work, we present the sequential resonance assignment of one of the polymorphs of Aβ(1-42) fibrils. We show that most of the protein is rigid, while a stretch of 4 residues (11-14) is not visible by solid-state NMR spectroscopy due to dynamics.

Keywords: Alzheimer’s disease; Amyloid fibrils; Amyloid-β peptide; Solid-state NMR spectroscopy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amyloid beta-Peptides / chemistry*
  • Nuclear Magnetic Resonance, Biomolecular*
  • Peptide Fragments / chemistry*
  • Protein Conformation, beta-Strand
  • Protein Multimerization*

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • amyloid beta-protein (1-42)