Production and use of recombinant Aβ for aggregation studies
(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:
https://lup.lub.lu.se/record/e399340f-74a9-49f7-abf5-6d790953e8bd
- author
- O’Malley, Tiernan T. ; Linse, Sara LU and Walsh, Dominic M.
- organization
- publishing date
- 2018-01-01
- 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
-
- pmid:29744844
- scopus:85046944871
- 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
- 2024-04-15 07:24:07
@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}},
keywords = {{Aggregation; Alzheimer’s disease; Amyloid β-protein; Dimer; Dityrosine; Fibrillogenesis; Monomer}},
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}},
}