Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic Resonance.
Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic Resonance.
复制标题
DOI：
10.1101/cshperspect.a024083
复制
发表时间：
2016-08-01
影响因子：
5.4
通讯作者：
Tycko R
中科院分区：
文献类型：
--
作者：
Tycko R
在体外和人脑组织中，淀粉样蛋白-β（Aβ）肽聚集形成多态性淀粉样蛋白原纤维和各种中间组装体，包括寡聚体和原纤维。进入世纪以来，对Aβ聚集体分子结构的研究取得了很大进展。已经为几种体外Aβ原纤维和一种亚稳态原纤维开发了主要基于固态核磁共振测量数据的完整分子结构模型。其他聚集中间体的部分结构表征已经实现。一个完整的结构模型的原纤维来源于脑组织也有报道。未来的工作可能会集中在脑组织的其他结构和进一步澄清非纤维状Aβ聚集体。
Amyloid-β (Aβ) peptides aggregate to form polymorphic amyloid fibrils and a variety of intermediate assemblies, including oligomers and protofibrils, both in vitro and in human brain tissue. Since the beginning of the 21st century, considerable progress has been made on characterization of the molecular structures of Aβ aggregates. Full molecular structural models that are based primarily on data from solid state nuclear magnetic resonance measurements have been developed for several in vitro Aβ fibrils and one metastable protofibril. Partial structural characterization of other aggregation intermediates has been achieved. One full structural model for fibrils derived from brain tissue has also been reported. Future work is likely to focus on additional structures from brain tissue and on further clarification of nonfibrillar Aβ aggregates.