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Related Experiment Video

Updated: Sep 7, 2025

Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans

Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans

Published on: November 26, 2017

Aging can transform single-component protein condensates into multiphase architectures.

Adiran Garaizar¹, Jorge R Espinosa¹, Jerelle A Joseph^1,2,3

¹Maxwell Centre, Cavendish Laboratory, Department of Physics, University of Cambridge, Cambridge CB3 0HE, United Kingdom.

Proceedings of the National Academy of Sciences of the United States of America

|June 21, 2022

Summary

Aging transforms single-component biomolecular condensates into multiphase structures. This study reveals how enhanced interprotein interactions during aging drive the formation of gel-core/liquid-shell or liquid-core/gel-shell architectures.

Keywords:

biomolecular condensates hollow condensates liquid–liquid phase separation multiscale modeling multiphase condensates

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Last Updated: Sep 7, 2025

Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans

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Published on: November 26, 2017

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

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4D Imaging of Protein Aggregation in Live Cells

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Published on: April 5, 2013

Area of Science:

Biophysics
Cell Biology
Soft Matter Physics

Background:

Biomolecular condensates with multiple phases are common in cells and in vitro.
Multiphase condensate formation depends on molecular diversity and solution conditions.
Condensate phase transformations can occur during aging.

Purpose of the Study:

Investigate thermodynamic factors driving single-component condensate transformation into multiphase architectures during aging.
Explain the progressive, intrinsic changes in condensates over time.
Explore the role of nonequilibrium aging processes.

Main Methods:

Developed a multiscale model integrating atomistic simulations, coarse-grained simulations, and a minimal aging model.
Performed nonequilibrium simulations of condensate aging.
Analyzed the effects of nonconservative intermolecular forces.

Main Results:

Predicted that initially homogeneous, liquid-like condensates transform into multiphase structures (gel-core/liquid-shell or liquid-core/gel-shell) as they age.
Showed this transformation is driven by gradual, irreversible enhancement of interprotein interactions.
Identified disorder-to-order transitions in prion-like domains as a potential mechanism for interaction enhancement.

Conclusions:

Aging can drive the spontaneous formation of multiphase biomolecular condensates from initially single-component systems.
The specific multiphase architecture depends on aging mechanisms, phase organization, and protein composition.
This work proposes a mechanism for how aging leads to complex, multiphase condensate structures in cells.