Kinetic analysis of amyloid formation
(2018) In Methods in Molecular Biology 1779. p.181-196- Abstract
The formation of amyloid fibrils is a central phenomenon in the progressive pathology of many neurodegenerative diseases, as well as in the fabrication of functional materials. Several different molecular processes acting in concert are responsible for the formation of amyloid fibrils from monomeric protein in solution. Here, we describe a method to determine which microscopic processes drive the overall formation of fibrils by using chemical kinetics in combination with systematic experimental datasets analysed in a global manner. We outline general concepts for obtaining suitable kinetic data and detail the key stages of data analysis, from quality control to the verification of a specific mechanism of aggregation.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/861f9621-8af7-419e-b7d3-34c3508f21df
- author
- Meisl, Georg ; Michaels, Thomas C.T. ; Linse, Sara LU and Knowles, Tuomas P.J.
- organization
- publishing date
- 2018-01-01
- type
- Chapter in Book/Report/Conference proceeding
- publication status
- published
- subject
- keywords
- Amyloid fibrils, Kinetic modeling, Molecular-level mechanism, Protein aggregation, Self-assembly
- host publication
- Methods in Molecular Biology
- series title
- Methods in Molecular Biology
- volume
- 1779
- pages
- 16 pages
- publisher
- Humana Press
- external identifiers
-
- pmid:29886534
- scopus:85048513546
- ISSN
- 1064-3745
- DOI
- 10.1007/978-1-4939-7816-8_12
- language
- English
- LU publication?
- yes
- id
- 861f9621-8af7-419e-b7d3-34c3508f21df
- date added to LUP
- 2018-07-03 11:50:30
- date last changed
- 2024-01-29 18:11:21
@inbook{861f9621-8af7-419e-b7d3-34c3508f21df,
abstract = {{<p>The formation of amyloid fibrils is a central phenomenon in the progressive pathology of many neurodegenerative diseases, as well as in the fabrication of functional materials. Several different molecular processes acting in concert are responsible for the formation of amyloid fibrils from monomeric protein in solution. Here, we describe a method to determine which microscopic processes drive the overall formation of fibrils by using chemical kinetics in combination with systematic experimental datasets analysed in a global manner. We outline general concepts for obtaining suitable kinetic data and detail the key stages of data analysis, from quality control to the verification of a specific mechanism of aggregation.</p>}},
author = {{Meisl, Georg and Michaels, Thomas C.T. and Linse, Sara and Knowles, Tuomas P.J.}},
booktitle = {{Methods in Molecular Biology}},
issn = {{1064-3745}},
keywords = {{Amyloid fibrils; Kinetic modeling; Molecular-level mechanism; Protein aggregation; Self-assembly}},
language = {{eng}},
month = {{01}},
pages = {{181--196}},
publisher = {{Humana Press}},
series = {{Methods in Molecular Biology}},
title = {{Kinetic analysis of amyloid formation}},
url = {{http://dx.doi.org/10.1007/978-1-4939-7816-8_12}},
doi = {{10.1007/978-1-4939-7816-8_12}},
volume = {{1779}},
year = {{2018}},
}