Thermodynamics of amyloid formation and the role of intersheet interactions
Irbäck, Anders LU
and Wessén, Jonas
LU
(2015)
In Journal of Chemical Physics
143(10).
- Abstract
- The self-assembly of proteins into beta-sheet-rich amyloid fibrils has been observed to occur with sigmoidal kinetics, indicating that the system initially is trapped in a metastable state. Here, we use a minimal lattice-based model to explore the thermodynamic forces driving amyloid formation in a finite canonical (NVT) system. By means of generalized-ensemble Monte Carlo techniques and a semi-analytical method, the thermodynamic properties of this model are investigated for different sets of intersheet interaction parameters. When the interactions support lateral growth into multi-layered fibrillar structures, an evaporation/condensation transition is observed, between a supersaturated solution state and a thermodynamically distinct... (More)
- The self-assembly of proteins into beta-sheet-rich amyloid fibrils has been observed to occur with sigmoidal kinetics, indicating that the system initially is trapped in a metastable state. Here, we use a minimal lattice-based model to explore the thermodynamic forces driving amyloid formation in a finite canonical (NVT) system. By means of generalized-ensemble Monte Carlo techniques and a semi-analytical method, the thermodynamic properties of this model are investigated for different sets of intersheet interaction parameters. When the interactions support lateral growth into multi-layered fibrillar structures, an evaporation/condensation transition is observed, between a supersaturated solution state and a thermodynamically distinct state where small and large fibril-like species exist in equilibrium. Intermediate-size aggregates are statistically suppressed. These properties do not hold if aggregate growth is one-dimensional. (C) 2015 AIP Publishing LLC. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8062392
- author
- Irbäck, Anders
LU
and Wessén, Jonas
LU
- organization
- publishing date
- 2015
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Chemical Physics
- volume
- 143
- issue
- 10
- article number
- 105104
- publisher
- American Institute of Physics (AIP)
- external identifiers
-
- wos:000361572900075
- pmid:26374063
- scopus:84941354016
- pmid:26374063
- ISSN
- 0021-9606
- DOI
- 10.1063/1.4930280
- language
- English
- LU publication?
- yes
- id
- 77378656-1285-4a00-8a6e-97cb5c9121f5 (old id 8062392)
- date added to LUP
- 2016-04-01 09:58:10
- date last changed
- 2023-01-01 23:58:33
@article{77378656-1285-4a00-8a6e-97cb5c9121f5,
abstract = {{The self-assembly of proteins into beta-sheet-rich amyloid fibrils has been observed to occur with sigmoidal kinetics, indicating that the system initially is trapped in a metastable state. Here, we use a minimal lattice-based model to explore the thermodynamic forces driving amyloid formation in a finite canonical (NVT) system. By means of generalized-ensemble Monte Carlo techniques and a semi-analytical method, the thermodynamic properties of this model are investigated for different sets of intersheet interaction parameters. When the interactions support lateral growth into multi-layered fibrillar structures, an evaporation/condensation transition is observed, between a supersaturated solution state and a thermodynamically distinct state where small and large fibril-like species exist in equilibrium. Intermediate-size aggregates are statistically suppressed. These properties do not hold if aggregate growth is one-dimensional. (C) 2015 AIP Publishing LLC.}},
author = {{Irbäck, Anders and Wessén, Jonas}},
issn = {{0021-9606}},
language = {{eng}},
number = {{10}},
publisher = {{American Institute of Physics (AIP)}},
series = {{Journal of Chemical Physics}},
title = {{Thermodynamics of amyloid formation and the role of intersheet interactions}},
url = {{http://dx.doi.org/10.1063/1.4930280}},
doi = {{10.1063/1.4930280}},
volume = {{143}},
year = {{2015}},
}