National Institute of Genetic Engineering and Biotechnology, Tehran, Iran,
Pharmaceutical Sciences Research Center, Shiraz University of Medical Sciences, Shiraz, Iran.
Int J Nanomedicine. 2019 Jan 23;14:799-808. doi: 10.2147/IJN.S190354. eCollection 2019.
Most of nanoparticles are nontoxic and have high absorption capability. Therefore, nanoparticles binding can effectively restrain fibrillation of β-amyloid and α-synuclein proteins and eventually prevent the toxicity of pathogenesis peptide of Alzheimer. Super paramagnetic iron oxide nanoparticles (SPIONs) contain iron oxide core which can be connected to a special part through magnetic coating.
In this study, the effect of SPIONs with different charges was simultaneously examined on the fibrillation of both β-amyloid and α-synuclein proteins by applying Thioflavin-T assay.
According to the results of the investigation on amyloid-fibrillation mechanism in both β-amyloids and α-synucleins, it was revealed that negatively-charged nanoparticles encoded to -COOH by dextran-coating were able to have a considerable absorption decrease from 17,000-12,000 after 320 minutes delay to lag phase and decrease in binding level of thioflavin-T particles to β-sheets.
The different concentrations of these nanoparticles and special coating of each particle had an effect on the kinetics of β-amyloid and α-synuclein fibrillations.
大多数纳米粒子是无毒的，并且具有很高的吸收能力。因此，纳米粒子结合可以有效地抑制β-淀粉样蛋白和α-突触核蛋白的纤维形成，最终防止阿尔茨海默病发病肽的毒性。超顺磁氧化铁纳米粒子（SPIONs）含有氧化铁核心，可以通过磁涂层与特殊部分连接。
在这项研究中，通过应用硫黄素-T 测定法，同时检查了带不同电荷的 SPIONs 对β-淀粉样蛋白和α-突触核蛋白纤维形成的影响。
根据对β-淀粉样蛋白和α-突触核蛋白中淀粉样纤维形成机制的研究结果表明，带负电荷的纳米粒子通过葡聚糖涂层编码为-COOH，在 320 分钟的延迟到滞后期和硫黄素-T 粒子与β-折叠结合水平的降低后，能够从 17000-12000 有相当大的吸收减少。
这些纳米粒子的不同浓度和每个粒子的特殊涂层对β-淀粉样蛋白和α-突触核蛋白纤维形成的动力学有影响。
