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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:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Chemical Physics
volume
143
issue
10
publisher
American Institute of Physics
external identifiers
  • wos:000361572900075
  • pmid:26374063
  • scopus:84941354016
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
2015-10-22 08:01:41
date last changed
2017-01-01 03:09:39
@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.},
  articleno    = {105104},
  author       = {Irbäck, Anders and Wessén, Jonas},
  issn         = {0021-9606},
  language     = {eng},
  number       = {10},
  publisher    = {American Institute of Physics},
  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},
  volume       = {143},
  year         = {2015},
}