Purification of recombinantly expressed and cytotoxic human amyloid-beta peptide 1-42

被引:11
|
作者
Wiesehan, Katja [1 ]
Funke, Susanne Aileen [1 ]
Fries, Miriam [1 ]
Willbold, Dieter [1 ]
机构
[1] Forschungszentrum Julich, D-52425 Julich, Germany
来源
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES | 2007年 / 856卷 / 1-2期
关键词
purification; amyloid-beta peptide; cytotoxicity; aggregation; Alzheimer's disease;
D O I
10.1016/j.jchromb.2007.06.003
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The amyloid cascade hypothesis assigns the amyloid-beta peptide (A beta) a central role in the pathogenesis of Alzheimer's disease (AD). Although there are strong efforts to biophysically characterize formation of A beta aggregates and fibrils, as well as their prevention, progress is still severly hampered by the availability of tens of milligrams of recombinant A beta(1-42). Here, we describe a reliable and easy procedure to recombinantly express and purify A beta(1-42), which is fully cytotoxic and able to form fibrils without any further refolding steps. The yield of the procedure is 5-8 mg of tag-less peptide per liter culture volume. (C) 2007 Elsevier B.V. All rights reserved.
引用
收藏
页码:229 / 233
页数:5
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