NMR characterization of the interaction of GroEL with amyloid β as a model ligand

FEBS Lett. 2013 Jun 5;587(11):1605-9. doi: 10.1016/j.febslet.2013.04.007. Epub 2013 Apr 18.


Here we report an NMR study on the substrate interaction modes of GroEL using amyloid β (Aβ) as a model ligand. We found that GroEL could suppress Aβ(1-40) amyloid formation by interacting with its two hydrophobic segments Leu17-Ala21 and Ala30-Val36, which involve key residues in fibril formation. The binding site of Aβ(1-40) was mapped on a pair of α-helices located in the GroEL apical domain. These results provide insights into chaperonin recognition of amyloidogenic proteins of pathological interest.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amyloid / chemistry
  • Amyloid beta-Peptides / chemistry*
  • Binding Sites
  • Chaperonin 60 / chemistry*
  • Escherichia coli Proteins / chemistry*
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Fragments / chemistry*
  • Peptide Mapping
  • Protein Interaction Domains and Motifs
  • Protein Multimerization
  • Protein Structure, Secondary


  • Amyloid
  • Amyloid beta-Peptides
  • Chaperonin 60
  • Escherichia coli Proteins
  • Peptide Fragments
  • amyloid beta-protein (1-40)