纤维
形态学(生物学)
化学
生物物理学
高定向热解石墨
过饱和度
热解炭
蛋白质聚集
淀粉样纤维
淀粉样蛋白(真菌学)
基质(水族馆)
原子力显微镜
化学工程
结晶学
淀粉样β
石墨
材料科学
纳米技术
生物化学
有机化学
病理
无机化学
工程类
地质学
海洋学
生物
医学
疾病
遗传学
热解
作者
Ya‐Ling Chiang,Yu‐Jen Chang,Yun‐Ru Chen,Ing‐Shouh Hwang
出处
期刊:Langmuir
[American Chemical Society]
日期:2020-12-22
卷期号:37 (1): 516-523
被引量:1
标识
DOI:10.1021/acs.langmuir.0c03215
摘要
The onset or progression of numerous neurodegenerative diseases occurs due to aggregation of proteins that ultimately form fibrils. The assembly and morphology of fibrils are susceptible to environmental factors. In this work, we used atomic force microscopy (AFM) to investigate the effects of dissolved nitrogen and oxygen molecules on the morphology of fibrils formed by a hydrophobic amyloid peptide implicated in amyotrophic lateral sclerosis, 15 repeats of glycine–alanine, on a highly oriented pyrolytic graphite substrate. We started with preformed fibril solutions that were then diluted with buffers of different gas conditions, resulting in the aggregation of the fibrils into different morphologies that were revealed by AFM after adsorption on the substrate. Straight fibrils were observed in both degassed and ambient buffers, but a stronger lateral association was seen in degassed buffers. Smaller and softer fibrils were observed in O2-supersaturated buffers, and plaque-like fibril aggregates of considerably large size were evident in N2-supersaturated buffers. In overnight incubation experiments, we observed changes in both the morphology and height of the fibril aggregates, and their evolution varied with different gas conditions. These findings indicate that the gas type and concentration affect the aggregation of amyloid fibrils and may facilitate the development of biomaterial applications and treatments for amyloid-related diseases.
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