# Thermodynamics of amyloid formation and the role of intersheet interactions

Source: [Thermodynamics of amyloid formation and the role of intersheet interactions](<https://www.sota2.com/research/paper/68fa32ca1e209131ce88abe3>)

Collection index: [llms.txt](<https://www.sota2.com/research/llms.txt>)

Data updated: 2025-10-24T19:41:19.139Z

Authors: Anders Irb\\"ack, Jonas Wess\\'en

Published: 2016-01-04T12:25:58.000Z

## 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.

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## Original sources and implementation

[Original paper](<https://arxiv.org/abs/1601.00478>)

[PDF](<https://arxiv.org/pdf/1601.00478.pdf>)
