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Anders Irbäck. Photo.

Anders Irbäck

Professor

Anders Irbäck. Photo.

Thermodynamics of amyloid formation and the role of intersheet interactions

Author

  • Anders Irbäck
  • Jonas Wessén

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
  • Theoretical Particle Physics

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