Transient formation of intermediate conformational states of amyloid-β peptide revealed by heteronuclear magnetic resonance spectroscopy

FEBS Lett. 2011 Apr 6;585(7):1097-102. doi: 10.1016/j.febslet.2011.03.014. Epub 2011 Mar 12.

Abstract

A detailed analysis of the NMR spectra of amyloid-β (Aβ) peptide revealed a decrease in signal intensity at higher temperature, due to a reversible conformational change of the molecule. Although peak intensity did not depend on peptide concentrations, the intensity in the region from D23 to A30 depended significantly on temperature. During the early stages of Aβ aggregation, each molecule might adopt transiently a turn conformation at around D23-A30, which converts mutually with a random coil. Stabilization of a turn by further conformational change and/or molecular association would lead to the formation of a "nucleus" for amyloid fibrils.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / metabolism
  • Nuclear Magnetic Resonance, Biomolecular*
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism
  • Protein Conformation
  • Protein Multimerization
  • Protein Structure, Secondary
  • Temperature
  • Water / chemistry

Substances

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