Solid-state NMR as a probe of amyloid fibril structure.
Solid-state NMR as a probe of amyloid fibril structure.
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DOI：
10.1016/s1367-5931(00)00123-x
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发表时间：
2000-10
影响因子：
7.8
通讯作者：
R. Tycko
中科院分区：
文献类型：
--
作者：
R. Tycko
淀粉样原纤维本质上是非结晶、不溶性、高分子量的肽和蛋白质聚集体，具有相当大的生物医学和生物物理学意义。固态核磁共振技术具有独特的能力，能够在特定的原子间距离和扭转角水平上为淀粉样原纤维提供高分辨率、位点特异性的结构约束。迄今为止，关于淀粉样原纤维的固态核磁共振研究的报道数量相对较少。这些研究解决了原纤维中β-折叠的超分子组织和原纤维中肽构象的问题，并集中在阿尔茨海默病的β-淀粉样肽上。预计在不久的将来，固态 NMR 对各种来源的淀粉样原纤维会有许多其他应用，因为这些系统非常适合该技术，并且引起了当前的广泛关注。
Amyloid fibrils are intrinsically noncrystalline, insoluble, high-molecular-weight aggregates of peptides and proteins, with considerable biomedical and biophysical significance. Solid-state NMR techniques are uniquely capable of providing high-resolution, site-specific structural constraints for amyloid fibrils, at the level of specific interatomic distances and torsion angles. So far, a relatively small number of solid-state NMR studies of amyloid fibrils have been reported. These have addressed issues about the supramolecular organization of β-sheets in the fibrils and the peptide conformation in the fibrils, and have concentrated on the β-amyloid peptide of Alzheimer’s disease. Many additional applications of solid-state NMR to amyloid fibrils from a variety of sources are anticipated in the near future, as these systems are ideally suited for the technique and are of widespread current interest.