Techniques to study amyloid fibril formation in vitro
Techniques to study amyloid fibril formation in vitro
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DOI：
10.1016/j.ymeth.2004.03.012
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发表时间：
2004-09-01
期刊：
影响因子：
4.8
通讯作者：
Nilsson, MR
中科院分区：
文献类型：
--
作者：
Nilsson, MR
淀粉样原纤维是肽或蛋白质的有序聚集体，其在结构上是纤维状的，并导致许多疾病的并发症（例如，2型糖尿病、阿尔茨海默病和原发性系统性淀粉样变性）。这些原纤维也可以在体外制备，并且有三个标准将蛋白质聚集体定义为淀粉样原纤维：用刚果红染色时的绿色双折射、原纤维形态和β-折叠二级结构。本综述的目的是描述用于研究体外淀粉样蛋白原纤维形成的技术，解决数据收集和解释中的常见错误，并对目前用于将蛋白聚集体分类为淀粉样蛋白原纤维的标准进行批判性审查进行讨论。(C)2004年爱思唯尔公司All rights reserved.
Amyloid fibrils are ordered aggregates of peptides or proteins that are fibrillar in structure and contribute to the complications of many diseases (e.g., type 2 diabetes mellitus, Alzheimer's disease, and primary systemic amyloidosis). These fibrils can also be prepared in vitro and there are three criteria that define a protein aggregate as an amyloid fibril: green birefringence upon staining with Congo Red, fibrillar morphology, and beta-sheet secondary structure. The purpose of this review is to describe the techniques used to study amyloid fibril formation in vitro, address common errors in the collection and interpretation of data, and open a discussion for a critical review of the criteria currently used to classify a protein aggregate as an amyloid fibril. (C) 2004 Elsevier Inc. All rights reserved.