The Effect of (-)-Epigallocatechin-3-Gallate on the Amyloid-β Secondary Structure.

ABSTRACT: Amyloid-β (Aβ) is a macromolecular structure of great interest because its misfolding and aggregation, along with changes in the secondary structure, have been correlated with its toxicity in various neurodegenerative diseases. Small drug-like molecules can modulate the amyloid secondary structure and therefore have raised significant interest in applications to active and passive therapies targeting amyloids. In this study, we investigate the interactions of epigallocatechin-3-gallate (EGCG), found in green tea, with Aβ polypeptides, using a combination of in vitro immuno-infrared sensor measurements, docking, molecular dynamics simulations, and ab initio calculations. We find that the interactions of EGCG are dominated by only a few residues in the fibrils, including hydrophobic π-π inte

SUBMITTER: Acharya A 

PROVIDER: S-EPMC7376235 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature