Impact of the Astaxanthin, Betanin, and EGCG Compounds on Small Oligomers of Amyloid Aβ40 Peptide

J Chem Inf Model. 2020 Mar 23;60(3):1399-1408. doi: 10.1021/acs.jcim.9b01074. Epub 2020 Mar 10.


There is experimental evidence that the astaxanthin, betanin, and epigallocatechin-3-gallate (EGCG) compounds slow down the aggregation kinetics and the toxicity of the amyloid-β (Aβ) peptide. How these inhibitors affect the self-assembly at the atomic level remains elusive. To address this issue, we have performed for each ligand atomistic replica exchange molecular dynamic (REMD) simulations in an explicit solvent of the Aβ11-40 trimer from the U-shape conformation and MD simulations starting from Aβ1-40 dimer and tetramer structures characterized by different intra- and interpeptide conformations. We find that the three ligands have similar binding free energies on small Aβ40 oligomers but very distinct transient binding sites that will affect the aggregation of larger assemblies and fibril elongation of the Aβ40 peptide.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides
  • Betacyanins*
  • Catechin / analogs & derivatives
  • Molecular Dynamics Simulation
  • Peptide Fragments*
  • Protein Multimerization
  • Xanthophylls


  • Amyloid beta-Peptides
  • Betacyanins
  • Peptide Fragments
  • Xanthophylls
  • Catechin
  • astaxanthine
  • epigallocatechin gallate