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首页> 外文期刊>International journal of biomedical nanoscience and nanotechnology >The impact of protein disulfide bonds on the amyloid fibril morphology
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The impact of protein disulfide bonds on the amyloid fibril morphology

机译：蛋白质二硫键对淀粉样蛋白原纤维形态的影响

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摘要

Amyloid fibrils are associated with many neurodegenerative diseases. Being formed from more than 20 different proteins that are functionally or structurally unrelated, amyloid fibrils share a common cross-p core structure. It is a well-accepted hypothesis that fibril biological activity and the associated toxicity vary with their morphology. Partial denaturation of a native protein usually precedes the initial stage of fibrillation, namely the nucleation process. Low pH and elevated temperature, typical conditions of amyloid fibril formation in vitro, resulted in partial denaturation of the proteins. Cleavage of disulfide bonds results typically in significant disruption of protein native structure and in the formation of the molten global state. Herein we report on a comparative investigation of fibril formation by apo-a-lactalbumin and its analog that contains only one of the four original disulfide bonds using deep UV resonance and non-resonance Raman spectroscopy and atomic force microscopy. Significant differences in the aggregation mechanism and the resulting fibril morphology were found.
机译：淀粉样蛋白原纤维与许多神经退行性疾病有关。淀粉样蛋白原纤维由20多种在功能或结构上不相关的蛋白质组成，它们具有共同的cross-p核心结构。一个公认的假说是原纤维的生物学活性和相关的毒性随其形态而变化。天然蛋白质的部分变性通常在原纤化的初始阶段之前，即成核过程。低pH值和高温是淀粉样蛋白原纤维体外形成的典型条件，导致蛋白质部分变性。二硫键的断裂通常导致蛋白质天然结构的显着破坏和熔融整体状态的形成。本文中，我们通过深紫外共振和非共振拉曼光谱以及原子力显微镜对载脂蛋白-乳清蛋白及其类似物仅包含四个原始二硫键之一的原纤维形成进行了比较研究。发现在聚集机理和所得原纤维形态上存在显着差异。

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