Interaction between soluble Aβ-(1-40) monomer and Aβ-(1-42) fibrils probed by paramagnetic relaxation enhancement

FEBS Lett. 2013 Mar 18;587(6):620-4. doi: 10.1016/j.febslet.2013.02.008. Epub 2013 Feb 15.

Abstract

The most common isoforms of amyloid-β (Aβ) proteins are composed of 40 or 42 amino acid residues. While Aβ-(1-40) is the predominant species, Aβ-(1-42) is more fibrillogenic and neurotoxic, suggesting that Aβ-(1-42) plays a critical role in the initiation of amyloid fibril formation. We investigated the mechanisms by which soluble Aβ-(1-40) associates with preformed Aβ-(1-42) seeds. A paramagnetic relaxation enhancement analysis showed that the Aβ-(1-40) monomer and Aβ-(1-42) seed interact via their C-terminal region in a parallel fashion, and the N-terminal part does not to contribute to the interaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Binding Sites
  • Chromatography, High Pressure Liquid
  • Humans
  • Magnetic Resonance Spectroscopy
  • Peptide Fragments / chemistry*
  • Protein Binding
  • Protein Structure, Secondary
  • Recombinant Proteins / chemistry
  • Solubility
  • Solutions
  • Spin Labels

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • Recombinant Proteins
  • Solutions
  • Spin Labels
  • amyloid beta-protein (1-40)
  • amyloid beta-protein (1-42)