{"title":"Gold nanoparticles with amyloid-β reduce neurocell cytotoxicity for the treatment and care of Alzheimer’s disease therapy","authors":"Qing Hong, Xinchun Jin, Chenheng Zhou, Jiahui Shao","doi":"10.1007/s13404-023-00327-1","DOIUrl":null,"url":null,"abstract":"<div><p>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<sub>1-42</sub>) 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<sub>1-42</sub>. In addition, cytotoxicity studies on PC 12 cells showed that Aβ<sub>1-42</sub> with AuNPs were less toxic than untreated oligomers Aβ<sub>1-42</sub> 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.</p></div>","PeriodicalId":55086,"journal":{"name":"Gold Bulletin","volume":null,"pages":null},"PeriodicalIF":2.2000,"publicationDate":"2023-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Gold Bulletin","FirstCategoryId":"5","ListUrlMain":"https://link.springer.com/article/10.1007/s13404-023-00327-1","RegionNum":4,"RegionCategory":"工程技术","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"Chemistry","Score":null,"Total":0}
引用次数: 0
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 (Aβ1-42) 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 Aβ1-42. In addition, cytotoxicity studies on PC 12 cells showed that Aβ1-42 with AuNPs were less toxic than untreated oligomers Aβ1-42 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.
期刊介绍:
Gold Bulletin is the premier international peer reviewed journal on the latest science, technology and applications of gold. It includes papers on the latest research advances, state-of-the-art reviews, conference reports, book reviews and highlights of patents and scientific literature. Gold Bulletin does not publish manuscripts covering the snthesis of Gold nanoparticles in the presence of plant extracts or other nature-derived extracts. Gold Bulletin has been published over 40 years as a multidisciplinary journal read by chemists, physicists, engineers, metallurgists, materials scientists, biotechnologists, surface scientists, and nanotechnologists amongst others, both within industry and academia. Gold Bulletin is published in Association with the World Gold Council.