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首页> 外文期刊>Journal of Molecular Biology >Amyloid aggregation on lipid bilayers and its impact on membrane permeability.
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Amyloid aggregation on lipid bilayers and its impact on membrane permeability.

机译：脂质双层上的淀粉样蛋白聚集及其对膜通透性的影响。

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摘要

Fibrillar protein aggregates (amyloids) are involved in several common pathologies, e.g., Alzheimer's disease and type II diabetes. Accumulating evidence suggests that toxicity in amyloid-related diseases originates from the deposition of protein aggregates on the cell membrane, which results in bilayer disruption and cell leakage. The molecular mechanism of damage to the membrane, however, is still obscure. To shed light on it we have performed coarse-grained molecular dynamics simulations of fibril-forming amphipathic peptides in the presence of lipid vesicles. The simulation results show that highly amyloidogenic peptides fibrillate on the surface of the vesicle, damaging the bilayer and promoting leakage. In contrast, the ordered aggregation of peptides with low amyloidogenicity is hindered by the vesicles. Remarkably, leakage from the vesicle is caused by growing aggregates, but not mature fibrils. The simulation results provide a basis for understanding the range of aggregation behavior that is observed in experiments with fibril-forming (poly)peptides.
机译：原纤维蛋白聚集体（淀粉样蛋白）涉及几种常见的病理学，例如阿尔茨海默氏病和II型糖尿病。越来越多的证据表明，淀粉样蛋白相关疾病的毒性源自蛋白质聚集体在细胞膜上的沉积，从而导致双层破坏和细胞渗漏。然而，膜受损的分子机理仍然不清楚。为了阐明这一点，我们在存在脂质囊泡的情况下对形成原纤维的两亲性肽进行了粗粒度的分子动力学模拟。模拟结果表明，高度淀粉样蛋白生成的肽在囊泡表面原纤化，破坏了双层并促进了渗漏。相反，具有低淀粉样变性的肽的有序聚集受到囊泡的阻碍。明显地，从囊泡中泄漏是由聚集体的生长引起的，而不是成熟的原纤维引起的。模拟结果为了解形成原纤维（多）肽的实验中观察到的聚集行为范围提供了基础。

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