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首页> 外文期刊>Journal of Molecular Biology >Direct visualisation of the beta-sheet structure of synthetic Alzheimer's amyloid.
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Direct visualisation of the beta-sheet structure of synthetic Alzheimer's amyloid.

机译：合成阿尔茨海默氏症淀粉样蛋白的β-折叠结构的直接可视化。

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摘要

Amyloid fibrils are a major pathological feature of Alzheimer's disease as well as other amyloidoses including the prion diseases. They are an unusual phenomenon, being made up of different, normally soluble proteins which undergo a profound conformational change and assemble to form very stable, insoluble fibrils which accumulate in the extracellular spaces. In Alzheimer's disease the amyloid fibrils are composed of the A beta protein. Knowledge of the structure of amyloid is essential for understanding the abnormal assembly and deposition of these fibrils and could lead to the rational design of therapeutic agents for their prevention or disaggregation. Here we reveal the core structure of an Alzheimer's amyloid fibril by direct visualisation using cryo-electron microscopy. Synthetic amyloid fibrils composed of A beta residues 11 to 25 and 1 to 42 were examined. The A beta (11-25) fibrils are clearly composed of beta-sheet structure that is observable as striations across the fibres. The beta-strands run perpendicular to the fibre axis and the projections show that the fibres are composed of beta-sheets with the strands in direct register. This observation has implications not only for the further understanding of amyloid, but also for the development of cryo-electron microscopy for direct visualisation of secondary structure.
机译：淀粉样蛋白原纤维是阿尔茨海默氏病以及包括a病毒病在内的其他淀粉样蛋白的主要病理特征。它们是不寻常的现象，由不同的通常可溶的蛋白质组成，这些蛋白质经过深刻的构象变化并组装形成非常稳定的不溶性原纤维，这些原纤维积聚在细胞外空间中。在阿尔茨海默氏病中，淀粉样蛋白原纤维由Aβ蛋白组成。淀粉样蛋白结构的知识对于理解这些原纤维的异常组装和沉积是必不可少的，并且可能导致合理设计用于预防或分解的治疗剂。在这里，我们通过使用冷冻电子显微镜的直接可视化揭示了阿尔茨海默氏症淀粉样蛋白原纤维的核心结构。检查了由Aβ残基11至25和1至42组成的合成淀粉样蛋白原纤维。 A beta（11-25）原纤维明显由β-折叠结构组成，可以观察到作为横跨纤维的条纹。 β链垂直于纤维轴延伸，并且投影显示，纤维由β片层组成，这些链直接对齐。该观察结果不仅对淀粉样蛋白有进一步的了解，而且对直接观察二级结构的冷冻电子显微镜的发展也具有重要意义。

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