乙酰胆碱酯酶
生物物理学
圆二色性
淀粉样蛋白(真菌学)
蛋白质聚集
化学
体外
纳米孔
阿切
肽
单体
纤维
生物化学
纳米技术
酶
生物
材料科学
聚合物
无机化学
有机化学
作者
Nandhini Subramanian,Brittany E. Watson,Chen-Zhong Li,Melissa A. Moss,Chang Liu
标识
DOI:10.1016/j.snr.2023.100170
摘要
Aggregation of amyloid-β peptide (Aβ) is hypothesized to be the primary cause of Alzheimer's disease (AD) progression. Aβ aggregation has been widely studied using conventional sensing tools like emission fluorescence, electron microscopy, mass spectroscopy, and circular dichroism. However, none of these techniques can provide cost-efficient, highly sensitive quantification of Aβ aggregation kinetics at the molecular level. Among the influences on Aβ aggregation of interest to disease progression is the acceleration of Aβ aggregation by acetylcholinesterase (AChE), which is present in the brain and inflicts the fast progression of disease due to its direct interaction with Aβ. In this work, we demonstrate the ability of a biological nanopore to map and quantify AChE accelerated aggregation of Aβ monomers to mixed oligomers and small soluble aggregates with single-molecule precision. This method will allow future work on testing direct and indirect effects of therapeutic drugs on AChE accelerated Aβ aggregation as well as disease prognosis.
科研通智能强力驱动
Strongly Powered by AbleSci AI