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Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...

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Synthesis of Multi-walled Carbon Nanotubes Modified with Silver Nanoparticles and Evaluation of Their Antibacterial Activities and Cytotoxic Properties

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Published on: May 10, 2018

银功能化碳点调节粉样蛋白聚合和微生物感染.

Chao Wang¹, Xu Shao¹, Xiuyun Cao¹

¹Department of Chemistry, School of Chemistry and Chemical Engineering, Northwestern Polytechnical University, 127 Youyi Road, Xi'an 710072, China. xinwang@nwpu.edu.cn.

|November 7, 2025

概括

这项研究引入了银功能化碳点 (Ag@TACDs) 作为一种新的阿尔茨海默病 (AD) 治疗方法. Ag@TACDs针对粉样蛋白聚合和微生物感染,提供了多方面的治疗方法.

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科学领域:

神经科学是一个神经科学.
材料科学材料科学材料科学
生物技术是生物技术.

背景情况:

阿尔茨海默病 (AD) 与粉样蛋白积累和微生物感染有关.
目前针对阿尔茨海默氏症的单一向疗法显示出有限的临床疗效.
需要一个多目标战略来解决AD的复杂病理.

研究的目的:

开发一种用于阿尔茨海默氏症的新型多目标治疗剂.
研究银功能化碳点 (Ag@TACDs) 对粉样蛋白聚合和微生物感染的疗效.
评估Ag@TACDs的生物相容性和细胞效应.

主要方法:

进行了体外实验,以评估Ag@TACDs对粉样β 42 (Aβ₄₂) 错误折叠和纤维脱聚合物的影响.
评估了Ag@TACDs对细菌感染的抗菌活性.
进行了细胞活力和细胞毒性测定,以确定生物相容性和对Aβ₄₂寡合体诱导毒性的影响.

主要成果:

在低度 (10μg mL-1) 中,Ag@TACDs显著抑制了Aβ₄₂错误折叠和脱聚合的成熟Aβ₄₂纤维.
Ag@TACDs显示出对抗细菌感染的强有力的抗微生物特性.
这种新药具有良好的生物相容性,增强了细胞活性,并减少了来自Aβ₄₂寡合体的细胞毒性.

结论:

Ag@TACDs代表了阿尔茨海默病治疗的有希望的多目标战略.
这种方法有效地针对AD的关键病理特征,包括粉样蛋白聚合和感染.
这些发现支持Ag@TACDs作为AD治疗的潜在多位抑制剂的发展.