Amyloid Fibrils: Formation, Polymorphism, and Inhibition
Amyloid Fibrils: Formation, Polymorphism, and Inhibition
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DOI：
10.1021/jz4027612
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发表时间：
2014-02-06
影响因子：
5.7
通讯作者：
Hard, Torleid
中科院分区：
文献类型：
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作者：
Hard, Torleid
具有跨β脊柱基本结构的淀粉样原纤维是肽和蛋白质的普遍且稳定的形式。最近的研究为我们理解原纤维形成机制以及淀粉样原纤维结构多态性的惊人多样性和持久性做出了重大贡献。还成功证明了如何设计分子以通过不同机制抑制不需要的淀粉样蛋白形成。这些领域的未来研究将包括研究初级成核机制和寡聚中间体的结构、次级成核事件（自催化）的一般作用、阐明淀粉样蛋白增殖中结构形态保存的机制和含义，以及研究很大程度上尚未探索的交叉播种现象，即一种物种的淀粉样蛋白原纤维诱导另一种物种形成淀粉样蛋白的现象。
Amyloid fibrils with cross-beta spine basic architectures are prevalent and stable forms of peptides and proteins. Recent research has provided significant contributions to our understanding of the mechanisms of fibril formation and to the surprising diversity and persistence of structural polymorphism in amyloid fibrils. There have also been successful demonstrations of how molecules can be engineered to inhibit unwanted amyloid formation by different mechanisms. Future research in these areas will include investigations of mechanisms for primary nucleation and the structure of oligomeric intermediates, the general role of secondary nucleation events (autocatalysis), elucidation of the mechanisms and implications of preservation of structural morphology in amyloid propagation, and research into the largely unexplored phenomenon of cross-seeding, by which amyloid fibrils of one species induce the formation of amyloid by another species.