Probing transient non-native states in amyloid beta fiber elongation by NMR

Chem Commun (Camb). 2019 Apr 11;55(31):4483-4486. doi: 10.1039/c9cc01067j.

Abstract

Using NMR to probe transient binding of Aβ1-40 monomers to fibers, we find partially bound conformations with the highest degree of interaction near F19-K28 and a lesser degree of interaction near the C-terminus (L34-G37). This represents a shift away from the KLVFFA recognition sequence (residues 16-21) currently used for inhibitor design.

MeSH terms

  • Amino Acid Sequence
  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / metabolism
  • Microscopy, Electron
  • Nuclear Magnetic Resonance, Biomolecular*
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism
  • Protein Aggregates
  • Sonication

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • Protein Aggregates
  • amyloid beta-protein (1-40)