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Production and use of recombinant Aβ for aggregation studies

O’Malley, Tiernan T. ; Linse, Sara LU and Walsh, Dominic M. (2018) In Methods in Molecular Biology 1777. p.307-320
Abstract

The amyloid β-protein (Aβ) is believed to play a central role in Alzheimer’s disease (AD) pathogenesis and there is great interest in understanding the process of Aβ aggregation, its underlying mechanism and the species generated during aggregation and their biological activity. Although Aβ has been studied for more than 30 years, analysis of its aggregation has been hampered by structural and chemical impurities. Here we provide a detailed protocol for the expression and purification of chemically and structurally homogeneous Aβ monomer. We also describe a method to produce covalent Aβ dimers linked by phenolic coupling of tyrosine residues.

Please use this url to cite or link to this publication:
author
; and
organization
publishing date
type
Chapter in Book/Report/Conference proceeding
publication status
published
subject
keywords
Aggregation, Alzheimer’s disease, Amyloid β-protein, Dimer, Dityrosine, Fibrillogenesis, Monomer
host publication
Methods in Molecular Biology
series title
Methods in Molecular Biology
volume
1777
pages
14 pages
publisher
Humana Press
external identifiers
  • scopus:85046944871
  • pmid:29744844
ISSN
1064-3745
DOI
10.1007/978-1-4939-7811-3_19
language
English
LU publication?
yes
id
e399340f-74a9-49f7-abf5-6d790953e8bd
date added to LUP
2018-05-28 14:17:00
date last changed
2021-10-06 01:01:26
@inbook{e399340f-74a9-49f7-abf5-6d790953e8bd,
  abstract     = {<p>The amyloid β-protein (Aβ) is believed to play a central role in Alzheimer’s disease (AD) pathogenesis and there is great interest in understanding the process of Aβ aggregation, its underlying mechanism and the species generated during aggregation and their biological activity. Although Aβ has been studied for more than 30 years, analysis of its aggregation has been hampered by structural and chemical impurities. Here we provide a detailed protocol for the expression and purification of chemically and structurally homogeneous Aβ monomer. We also describe a method to produce covalent Aβ dimers linked by phenolic coupling of tyrosine residues.</p>},
  author       = {O’Malley, Tiernan T. and Linse, Sara and Walsh, Dominic M.},
  booktitle    = {Methods in Molecular Biology},
  issn         = {1064-3745},
  language     = {eng},
  month        = {01},
  pages        = {307--320},
  publisher    = {Humana Press},
  series       = {Methods in Molecular Biology},
  title        = {Production and use of recombinant Aβ for aggregation studies},
  url          = {http://dx.doi.org/10.1007/978-1-4939-7811-3_19},
  doi          = {10.1007/978-1-4939-7811-3_19},
  volume       = {1777},
  year         = {2018},
}