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Protein droplets in systems of disordered homopeptides and the amyloid glass phase

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Abstract

In order to gain insight into the formation of proteinaceous liquid droplets, we study systems of many disordered homopeptide chains within our coarse-grained molecular dynamics model with conformation-dependent terms. We construct the phase diagrams for polyalanine of length 20 and polyglutamines of lengths 20, 40 and 60 based on the stationary-state cluster distribution. The phase diagrams are distinct but correspond to the same topology. We delineate the liquid–gas coexistence curve at around room temperature. We also identify a novel amyloid glass phase that is substantially cross linked forming amorphous and anisotropic spatial patterns. Generally, this phase is found at lower temperatures, but may also appear at room temperature for sufficiently long chains. We demonstrate the existence of fluid-like phenomena, like droplet fusion and fission. However, our available length scales have not yet shown the validity of the continuum physics description.

Graphical abstract: Protein droplets in systems of disordered homopeptides and the amyloid glass phase

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Article information


Submitted
26 Mar 2020
Accepted
01 Jun 2020
First published
03 Jun 2020

Phys. Chem. Chem. Phys., 2020, Advance Article
Article type
Paper

Protein droplets in systems of disordered homopeptides and the amyloid glass phase

Ł. Mioduszewski and M. Cieplak, Phys. Chem. Chem. Phys., 2020, Advance Article , DOI: 10.1039/D0CP01635G

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