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Anders Irbäck
Professor
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Thermodynamics of amyloid formation and the role of intersheet interactions
Author
Summary, in English
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.
Department/s
- Computational Biology and Biological Physics - Has been reorganised
- Theoretical Particle Physics - Has been reorganised
Publishing year
2015
Language
English
Publication/Series
Journal of Chemical Physics
Volume
143
Issue
10
Document type
Journal article
Publisher
American Institute of Physics (AIP)
Topic
- Other Physics Topics
- Biophysics
Status
Published
ISBN/ISSN/Other
- ISSN: 0021-9606