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Updated: Sep 19, 2025

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Controlling Multiphase Coacervate Wetting and Self-Organization by Interfacial Proteins.

Tiemei Lu1,2, Susanne Liese3, Brent S Visser1

  • 1Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, Nijmegen 6525 AJ, The Netherlands.

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Summary
This summary is machine-generated.

Surface-active proteins like alpha-synuclein (αSyn) control the organization of multiphase biomolecular condensates. Introducing αSyn transforms nested droplets into connected networks, forming dynamic "coacervate polymers" with implications for cellular organization.

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Area of Science:

  • Cellular biology
  • Biophysics
  • Materials science

Background:

  • Biomolecular condensates organize cellular processes and often exhibit multiphase architectures.
  • Regulation of transformations between multiphase architectures in cells is poorly understood.

Purpose of the Study:

  • To investigate how surface-active proteins influence wetting and self-organization in multiphase coacervates.
  • To understand the role of interfacial proteins in regulating condensate architecture and interactions.

Main Methods:

  • Utilized multiphase coacervates (UTP/pLL/R10) as model systems.
  • Introduced surface-active protein alpha-synuclein (αSyn) to study its effect on coacervate interfaces.
  • Developed a theoretical model to explain the observed wetting transitions.

Main Results:

  • αSyn induced a transition from nested to partially wetted droplets in multiphase coacervates.
  • Partially wetted droplets formed dynamic, stable networks resembling polymers ("coacervate polymers").
  • Diverse proteins (BSA, mCherry, FtsZ) demonstrated similar surface activity and organizational effects.

Conclusions:

  • Interfacial proteins can control multiphase condensate organization and inter-condensate interactions.
  • This mechanism may be crucial for cellular regulation of condensate stability and network formation.
  • Findings suggest a general principle for protein-mediated control over condensate architecture.