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Visualizing Super-Diffusion, Oligomerization, and Fibrillation of Amyloid-β Peptide Chains along Tubular Membranes
ACS Macro Letters ( IF 5.8 ) Pub Date : 2021-10-04 , DOI: 10.1021/acsmacrolett.1c00541
Yuhang Song 1 , Yu Geng 1 , Lei Shen 1
Affiliation  

A deeper mechanistic study of peptide amyloidosis on lipid membranes with varying shapes could enhance the comprehensive understanding of the contribution of cellular structures to multiple neurodegenerative diseases, including Alzheimer’s disease. We report here the direct visual observation of amyloid-β peptide (Aβ) superdiffusing along tubular lipid membranes via single-molecule tracking (SMT). Such mobility on tubular membranes is critical, as it allows Aβ chains to oligomerize and elongate into fibrils. Factors such as cholesterol that favor Aβ chains with sufficient surface residence time can promote the inter-Aβ interaction and enhance Aβ fibrillation. This study provides previously uncharacterized insights into the chain behaviors of Aβ along important biological nanowire structures, which is essential to understanding and exploring the factors of cellular shapes to manipulate peptide amyloidosis.

中文翻译:

可视化淀粉样蛋白-β 肽链沿管状膜的超扩散、寡聚化和原纤维化

对不同形状的脂质膜上的肽淀粉样变性进行更深入的机制研究,可以增强对细胞结构对包括阿尔茨海默病在内的多种神经退行性疾病的贡献的全面理解。我们在此报告通过单分子追踪 (SMT) 沿管状脂质膜超扩散的淀粉样蛋白-β 肽 (Aβ) 的直接视觉观察。这种在管状膜上的移动性至关重要,因为它允许 Aβ 链低聚并伸长成原纤维。胆固醇等有利于具有足够表面停留时间的 Aβ 链的因素可以促进 Aβ 间的相互作用并增强 Aβ 纤维化。这项研究为 Aβ 沿着重要的生物纳米线结构的链行为提供了以前未表征的见解,
更新日期:2021-10-19
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