The liquid structure of elastin

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Abstract

The protein elastin imparts extensibility, elastic recoil, and resilience to tissues including arterial walls, skin, lung alveoli, and the uterus. Elastin and elastin-like peptides are hydrophobic, disordered, and undergo liquid-liquid phase separation upon self-assembly. Despite extensive study, the structure of elastin remains controversial. We use molecular dynamics simulations on a massive scale to elucidate the structural ensemble of aggregated elastin-like peptides. Consistent with the entropic nature of elastic recoil, the aggregated state is stabilized by the hydrophobic effect. However, self-assembly does not entail formation of a hydrophobic core. The polypeptide backbone forms transient, sparse hydrogen-bonded turns and remains significantly hydrated even as self-assembly triples the extent of non-polar side-chain contacts. Individual chains in the assembly approach a maximally-disordered, melt-like state which may be called the liquid state of proteins. These findings resolve long-standing controversies regarding elastin structure and function and afford insight into the phase separation of disordered proteins.

Data availability

The following data sets were generated

1. S Rauscher and R Pomès
(2017) Microsecond-long molecular dynamics trajectory of an aggregate of elastin-like peptides in water
Available at Figshare under a CC BY 4.0 License.

https://doi.org/10.6084/m9.figshare.5532214.v1

Article and author information

Author details

Sarah Rauscher

Molecular Structure and Function, The Hospital for Sick Children, Toronto, Canada

Competing interests
The authors declare that no competing interests exist.
Régis Pomès

Molecular Structure and Function, The Hospital for Sick Children, Toronto, Canada

For correspondence
pomes@sickkids.ca

Competing interests
The authors declare that no competing interests exist.

"This ORCID iD identifies the author of this article:" 0000-0003-3068-9833

Funding

Canadian Institutes of Health Research (MOP84496)

Régis Pomès

Natural Sciences and Engineering Research Council of Canada

Sarah Rauscher

Hospital for Sick Children

Sarah Rauscher

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.

Copyright

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.