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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Stepwise dynamics of epitaxially growing single amyloid fibrils
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Stepwise dynamics of epitaxially growing single amyloid fibrils

机译：外延生长的单个淀粉样原纤维的逐步动力学

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摘要

The assembly mechanisms of amyloid fibrils, tissue deposits in a variety of degenerative diseases, is poorly understood. With a simply modified application of the atomic force microscope, we monitored the growth, on mica surface, of individual fibrils of the amyloid β25-35 peptide with near-subunit spatial and subsecond temporal resolution. Fibril assembly was polarized and discontinuous. Bursts of rapid (up to 300-nm~(-1)) growth phases that extended the fibril by ≈7 nm or its integer multiples were interrupted with pauses. Stepwise dynamics were also observed for amyloid β1-42 fibrils growing on graphite, suggesting that the discontinuous assembly mechanisms may be a general feature of epitaxial amyloid growth. Amyloid assembly may thus involve fluctuation between a fast-growing and a blocked state in which the fibril is kinetically trapped because of intrinsic structural features. The used scanning-force kymography method may be adapted to analyze the assembly dynamics of a wide range of linear biopolymers.
机译：淀粉样蛋白原纤维的组装机制，各种退行性疾病中的组织沉积，了解得很少。通过原子力显微镜的简单修改应用，我们以接近亚单位的空间和亚秒级的时间分辨率监测了淀粉样蛋白β25-35肽的单个原纤维在云母表面的生长。原纤维组件极化且不连续。将原纤维延长到≈7nm或其整数倍的快速（高达300 nm〜（-1））生长期的爆发被暂停而中断。还观察到了在石墨上生长的淀粉样β1-42原纤维的逐步动力学，这表明不连续的组装机制可能是外延淀粉样蛋白生长的一般特征。因此，淀粉样蛋白组装可能涉及快速生长和封闭状态之间的波动，在该状态中，由于固有的结构特征，原纤维被动态地捕获。所使用的扫描力运动方法可以适于分析各种线性生物聚合物的组装动力学。

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