Thermodynamics of amyloid formation and the role of intersheet interactions

Research output: Contribution to journalArticle


title = "Thermodynamics of amyloid formation and the role of intersheet interactions",
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 = "Anders Irb{\"a}ck and Jonas Wess{\'e}n",
year = "2015",
doi = "10.1063/1.4930280",
language = "English",
volume = "143",
journal = "Journal of Chemical Physics",
issn = "0021-9606",
publisher = "American Institute of Physics",
number = "10",