体外研究淀粉样纤维形成的技术。

Techniques to study amyloid fibril formation in vitro.

作者信息

Nilsson Melanie R

机构信息

Department of Chemistry, McDaniel College, Eaton Hall, 2 College Hill, Westminster, MD 21157, USA.

出版信息

Methods. 2004 Sep;34(1):151-60. doi: 10.1016/j.ymeth.2004.03.012.

DOI:10.1016/j.ymeth.2004.03.012

PMID:15283924

Abstract

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.

摘要

淀粉样纤维是肽或蛋白质的有序聚集体，其结构呈纤维状，并导致许多疾病（如2型糖尿病、阿尔茨海默病和原发性系统性淀粉样变性）的并发症。这些纤维也可以在体外制备，有三个标准将蛋白质聚集体定义为淀粉样纤维：用刚果红染色后呈现绿色双折射、纤维形态以及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纤维形成的技术，指出数据收集和解释中的常见错误，并展开讨论，对目前用于将蛋白质聚集体分类为淀粉样纤维的标准进行批判性审视。