A comparative analysis of the aggregation behavior of amyloid-β peptide variants

被引：61

作者：

Vandersteen, Annelies ^{[1
,2
]}

Hubin, Ellen ^{[1
,3
,4
]}

Sarroukh, Rabia ^{[5
]}

De Baets, Greet ^{[2
]}

Schymkowitz, Joost ^{[2
]}

Rousseau, Frederic ^{[2
]}

Subramaniam, Vinod ^{[1
]}

Raussens, Vincent ^{[5
]}

Wenschuh, Holger ^{[6
]}

Wildemann, Dirk ^{[6
]}

Broersen, Kerensa ^{[1
]}

机构：

[1] Univ Twente, Nanobiophys Grp, MIRA Inst Biomed Technol & Tech Med, Fac Sci & Technol, NL-7500 AE Enschede, Netherlands

[2] Katholieke Univ Leuven KUL, VIB Switch Lab, Dept Cellular & Mol Med, B-3000 Louvain, Belgium

[3] Vrije Univ Brussel VUB, Dept Biotechnol DBIT, B-1050 Brussels, Belgium

[4] VIB Dept Struct Biol, B-1050 Brussels, Belgium

[5] Univ Libre Bruxelles, Ctr Struct Biol & Bioinformat, Lab Struct & Funct Biol Membranes, B-1050 Brussels, Belgium

[6] JPT Peptide Technol GmbH, D-12489 Berlin, Germany

来源：

FEBS LETTERS | 2012年 / 586卷 / 23期

关键词：

Thioflavin T fluorescence; Alzheimer's disease; FAD mutation; Biotinylation; p3; Peptide; Biophysics; TRANSMEMBRANE DOMAIN; ALZHEIMERS-DISEASE; PROTEIN; MUTATIONS; SECRETASE; CLEAVAGE; NEUROTOXICITY; PATHOGENESIS; DEGRADATION; PREDICTION;

D O I：

10.1016/j.febslet.2012.10.022

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Aggregated forms of the amyloid-beta peptide are hypothesized to act as the prime toxic agents in Alzheimer disease (AD). The in vivo amyloid-beta peptide pool consists of both C- and N-terminally truncated or mutated peptides, and the composition thereof significantly determines AD risk. Other variations, such as biotinylation, are introduced as molecular tools to aid the understanding of disease mechanisms. Since these modifications have the potential to alter key aggregation properties of the amyloid-beta peptide, we present a comparative study of the aggregation of a substantial set of the most common in vivo identified and in vitro produced amyloid-beta peptides.

引用

页码：4088 / 4093

页数：6

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