Gold nanoparticles with amyloid-β reduce neurocell cytotoxicity for the treatment and care of Alzheimer’s disease therapy

Abstract

Protein oligomerization contributes to Alzheimer’s disease development (AD). A nanoparticle that can speed up the oligomerization of proteins is generally considered harmful. Gold nanoparticles (AuNPs) have been reported to be making headway in biological platforms, but they may also have the capacity to stimulate protein oligomerization. Our goal herein was to investigate the neurotoxicity and oligomerization of amyloid-β-1-42 (Aβ_1-42) in the presence of AuNPs. The precipitation approach was used to create AuNPs, which were then analyzed using transmission electron microscopy (TEM), ThT, Congo red, and CD spectroscopy. The results demonstrated that the 50-nm-sized fabricated AuNPs guided acceleration in Aβ_1-42. In addition, cytotoxicity studies on PC 12 cells showed that Aβ_1-42 with AuNPs were less toxic than untreated oligomers Aβ_1-42 in terms of inducing cell death, oxidative apoptosis, stress, and membrane leakage. In conclusion, our investigation sheds light on how AuNPs stimulate the development of cytotoxic oligomers by binding to proteins in Alzheimer’s disease.