Toward the equilibrium and kinetics of amyloid peptide self-assembly
(2021) In Current Opinion in Structural Biology 70. p.87-98- Abstract
Several devastating human diseases are linked to peptide self-assembly, but our understanding their onset and progression is not settled. This is a sign of the complexity of the aggregation process, which is prevented, catalyzed, or retarded by numerous factors in body fluids and cells, varying in time and space. Biophysical studies of pure peptide solutions contribute insights into the underlying steps in the process and quantitative parameters relating to rate constants (energy barriers) and equilibrium constants (population distributions). This requires methods to quantify the concentration of at least one species in the process. Translation to an in vivo situation poses an enormous challenge, and the effects of selected components... (More)
Several devastating human diseases are linked to peptide self-assembly, but our understanding their onset and progression is not settled. This is a sign of the complexity of the aggregation process, which is prevented, catalyzed, or retarded by numerous factors in body fluids and cells, varying in time and space. Biophysical studies of pure peptide solutions contribute insights into the underlying steps in the process and quantitative parameters relating to rate constants (energy barriers) and equilibrium constants (population distributions). This requires methods to quantify the concentration of at least one species in the process. Translation to an in vivo situation poses an enormous challenge, and the effects of selected components (bottom up) or entire body fluids (top down) need to be quantified.
(Less)
- author
- Linse, Sara LU
- organization
- publishing date
- 2021-10-01
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Current Opinion in Structural Biology
- volume
- 70
- pages
- 12 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:85109088619
- pmid:34153659
- ISSN
- 0959-440X
- DOI
- 10.1016/j.sbi.2021.05.004
- language
- English
- LU publication?
- yes
- additional info
- Funding Information: This work was supported by the Swedish Research Council, VR (2015-00143).
- id
- 7d9c8595-c2a2-4403-aef7-59d525b7b5ce
- date added to LUP
- 2021-08-16 12:53:49
- date last changed
- 2024-06-15 14:25:24
@article{7d9c8595-c2a2-4403-aef7-59d525b7b5ce,
abstract = {{<p>Several devastating human diseases are linked to peptide self-assembly, but our understanding their onset and progression is not settled. This is a sign of the complexity of the aggregation process, which is prevented, catalyzed, or retarded by numerous factors in body fluids and cells, varying in time and space. Biophysical studies of pure peptide solutions contribute insights into the underlying steps in the process and quantitative parameters relating to rate constants (energy barriers) and equilibrium constants (population distributions). This requires methods to quantify the concentration of at least one species in the process. Translation to an in vivo situation poses an enormous challenge, and the effects of selected components (bottom up) or entire body fluids (top down) need to be quantified.</p>}},
author = {{Linse, Sara}},
issn = {{0959-440X}},
language = {{eng}},
month = {{10}},
pages = {{87--98}},
publisher = {{Elsevier}},
series = {{Current Opinion in Structural Biology}},
title = {{Toward the equilibrium and kinetics of amyloid peptide self-assembly}},
url = {{http://dx.doi.org/10.1016/j.sbi.2021.05.004}},
doi = {{10.1016/j.sbi.2021.05.004}},
volume = {{70}},
year = {{2021}},
}