Techniques to study amyloid fibril formation in vitro

被引：814

作者：

Nilsson, MR ^{[1
]}

机构：

[1] McDaniel Coll, Dept Chem, Westminster, MD 21157 USA

来源：

METHODS | 2004年 / 34卷 / 01期

关键词：

amyloid fibrils; protein aggregation; Congo Red; FTIR; TEM; criteria; classification; review; techniques; thioflavin T;

D O I：

10.1016/j.ymeth.2004.03.012

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：151 / 160

页数：10

共 64 条

[51] The amyloidogenicity of gelsolin is controlled by proteolysis and pH [J].