Impact of the Astaxanthin, Betanin, and EGCG Compounds on Small Oligomers of Amyloid Aβ40Peptide

Huynh Minh Hung, Minh Tho Nguyen, Phuong Thao Tran, Vi Khanh Truong, James Chapman, Le Huu Quynh Anh, Philippe Derreumaux, Van V. Vu, Son Tung Ngo

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1399-1408
Number of pages10
JournalJournal of Chemical Information and Modeling
Volume60
Issue number3
DOIs
Publication statusPublished - 23 Mar 2020
Externally publishedYes

Keywords

  • Astaxanthin
  • Betanin
  • Amyloid Aβ40 Peptide

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