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

TitleImpact of the Astaxanthin, Betanin, and EGCG Compounds on Small Oligomers of Amyloid Aβ Peptide.
Publication TypeJournal Article
Year of Publication2020
AuthorsHung HMinh, Nguyen MTho, Tran P-T, Truong VKhanh, Chapman J, Anh LHuu Quynh, Derreumaux P, Vu VV, Ngo STung
JournalJ Chem Inf Model
Volume60
Issue3
Pagination1399-1408
Date Published2020 Mar 23
ISSN1549-960X
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 Aβ trimer from the U-shape conformation and MD simulations starting from Aβ dimer and tetramer structures characterized by different intra- and interpeptide conformations. We find that the three ligands have similar binding free energies on small Aβ oligomers but very distinct transient binding sites that will affect the aggregation of larger assemblies and fibril elongation of the Aβ peptide.

DOI10.1021/acs.jcim.9b01074
Alternate JournalJ Chem Inf Model
Citation Key2020|2125
PubMed ID32105466