Facile synthesis of EGCG modified Au nanoparticles and their inhibitory effects on amyloid protein aggregation

Int J Biol Macromol. 2024 Nov;281(Pt 4):136501. doi: 10.1016/j.ijbiomac.2024.136501. Epub 2024 Oct 10.

Abstract

Preventing β-amyloid (Aβ) peptide aggregation by Au nanoparticles (NPs) is a promising strategy for the treatment of Alzheimer's disease. However, construction of Au nanostructures with easy preparation and high therapeutic efficiency is still a challenge. Herein, one-step pulsed laser ablation in water is used to fabricate epigallocatechin-3-gallate (EGCG) modified Au (Au-EGCG) NPs with uniform size. The as-obtained Au-EGCG NPs can effectively inhibit β-amyloid (1-42) peptide (Aβ42) aggregation by the interaction with peptides, which is confirmed by transmission electron microscopy (TEM), fluorescence spectroscopy (thioflavin T (ThT), tyrosine and 8-anilinonaphthalene-1-sulfonic acid (ANS) assays), and Fourier transform infrared (FT-IR) spectroscopy. Besides, they can also effectively attenuate Aβ42-induced cytotoxicity based on the cell viability experiments. This work provides a facile approach to synthesize the surface-functionalized Au NPs for enhanced inhibition of Aβ aggregation and amelioration of Aβ-induced cytotoxicity.

Keywords: Alzheimer's disease; Amyloid protein; Au nanoparticles; Epigallocatechin-3-gallate; Pulsed laser ablation.

MeSH terms

  • Amyloid beta-Peptides* / antagonists & inhibitors
  • Amyloid beta-Peptides* / chemistry
  • Amyloid beta-Peptides* / metabolism
  • Catechin* / analogs & derivatives
  • Catechin* / chemical synthesis
  • Catechin* / chemistry
  • Catechin* / pharmacology
  • Cell Survival / drug effects
  • Gold* / chemistry
  • Humans
  • Metal Nanoparticles* / chemistry
  • Peptide Fragments / chemistry
  • Peptide Fragments / pharmacology
  • Protein Aggregates / drug effects

Substances

  • Gold
  • Catechin
  • epigallocatechin gallate
  • Amyloid beta-Peptides
  • Protein Aggregates
  • amyloid beta-protein (1-42)
  • Peptide Fragments