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

Annelies Vandersteen; Ellen Hubin; Rabia Sarroukh; Greet De Baets; Joost Schymkowitz; Frederic Rousseau; Vinod Subramaniam; Vincent Raussens; Holger Wenschuh; Dirk Wildemann; Kerensa Broersen

doi:10.1016/j.febslet.2012.10.022

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

Annelies Vandersteen, Ellen Hubin, Rabia Sarroukh, Greet De Baets, Joost Schymkowitz, Frederic Rousseau, Vinod Subramaniam, Vincent Raussens, Holger Wenschuh, Dirk Wildemann, Kerensa Broersen

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

Aggregated forms of the amyloid-β peptide are hypothesized to act as the prime toxic agents in Alzheimer disease (AD). The in vivo amyloid-β 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-β 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-β peptides.

Original language	English
Pages (from-to)	4088-93
Number of pages	6
Journal	FEBS Letters
Volume	586
Issue number	23
DOIs	https://doi.org/10.1016/j.febslet.2012.10.022
Publication status	Published - 30 Nov 2012

Keywords

Amyloid beta-Peptides
Biotinylation
Microscopy, Electron, Transmission
Spectroscopy, Fourier Transform Infrared
Journal Article
Research Support, Non-U.S. Gov't

Access to Document

10.1016/j.febslet.2012.10.022

Persistent URL (handle)

Persistent link

Cite this

@article{1f81a7d30bf444b99c6695a325342657,

title = "A comparative analysis of the aggregation behavior of amyloid-β peptide variants",

abstract = "Aggregated forms of the amyloid-β peptide are hypothesized to act as the prime toxic agents in Alzheimer disease (AD). The in vivo amyloid-β 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-β 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-β peptides.",

keywords = "Amyloid beta-Peptides, Biotinylation, Microscopy, Electron, Transmission, Spectroscopy, Fourier Transform Infrared, Journal Article, Research Support, Non-U.S. Gov't",

author = "Annelies Vandersteen and Ellen Hubin and Rabia Sarroukh and {De Baets}, Greet and Joost Schymkowitz and Frederic Rousseau and Vinod Subramaniam and Vincent Raussens and Holger Wenschuh and Dirk Wildemann and Kerensa Broersen",

year = "2012",

month = nov,

day = "30",

doi = "10.1016/j.febslet.2012.10.022",

language = "English",

volume = "586",

pages = "4088--93",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

number = "23",

}

TY - JOUR

T1 - A comparative analysis of the aggregation behavior of amyloid-β peptide variants

AU - Vandersteen, Annelies

AU - Hubin, Ellen

AU - Sarroukh, Rabia

AU - De Baets, Greet

AU - Schymkowitz, Joost

AU - Rousseau, Frederic

AU - Subramaniam, Vinod

AU - Raussens, Vincent

AU - Wenschuh, Holger

AU - Wildemann, Dirk

AU - Broersen, Kerensa

PY - 2012/11/30

Y1 - 2012/11/30

N2 - Aggregated forms of the amyloid-β peptide are hypothesized to act as the prime toxic agents in Alzheimer disease (AD). The in vivo amyloid-β 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-β 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-β peptides.

AB - Aggregated forms of the amyloid-β peptide are hypothesized to act as the prime toxic agents in Alzheimer disease (AD). The in vivo amyloid-β 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-β 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-β peptides.

KW - Amyloid beta-Peptides

KW - Biotinylation

KW - Microscopy, Electron, Transmission

KW - Spectroscopy, Fourier Transform Infrared

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1016/j.febslet.2012.10.022

DO - 10.1016/j.febslet.2012.10.022

M3 - Article

C2 - 23103738

SN - 0014-5793

VL - 586

SP - 4088

EP - 4093

JO - FEBS Letters

JF - FEBS Letters

IS - 23

ER -

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

Abstract

Keywords

Access to Document

Persistent URL (handle)

Fingerprint

Cite this