Related Experiment Video
Updated: Jun 10, 2025
Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
Published on: March 21, 2025
Facile synthesis of EGCG modified Au nanoparticles and their inhibitory effects on amyloid protein aggregation
Ting Wu1, Yufei Zhang2, Haolin Li2
1CAS Key Lab for Biomedical Effects of Nanomaterials and Nanosafety, Center of Materials Science and Optoelectronics Engineering, CAS Center for Excellence in Nanoscience, National Center for Nanoscience and Technology, University of Chinese Academy of Sciences, Beijing 100190, China.
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.
