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Stabilization of Condensate Interfaces Using Dynamic Protein Insertion.

Yannick H A Leurs1,2,3, Sanne N Giezen4,3, Yudong Li2,3

  • 1Laboratory of Chemical Biology, Department of Biomedical Engineering, Eindhoven University of Technology, Eindhoven, 5612 AZ, The Netherlands.

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Summary
This summary is machine-generated.

Engineered proteins stabilize polypeptide coacervates, mimicking cellular membraneless organelles (MLOs). This protein layer prevents coacervate dissolution and fusion, offering insights into MLO stability.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Materials Science

Background:

  • Coacervates are used to model membraneless organelles (MLOs).
  • Unstabilized coacervates lack the robustness of natural MLOs.
  • Surface-active proteins are key to stabilizing coacervate systems.

Purpose of the Study:

  • To engineer surface-active proteins for coacervate stabilization.
  • To investigate the role of protein dimerization in coacervate stability.
  • To understand the dynamic interactions at the coacervate-liquid interface.

Main Methods:

  • Utilized engineered surface-active proteins to stabilize polypeptide coacervates.
  • Employed Cryo-Transmission Electron Microscopy (Cryo-TEM) for interface imaging.
  • Applied single-molecule super-resolution microscopy to observe protein dynamics.

Main Results:

  • Engineered proteins formed a stable monolayer at the coacervate interface, preventing dissolution and fusion.
  • Protein dimerization was identified as crucial for effective interface stabilization.
  • Proteins exhibited rapid (un)docking and movement at the interface within milliseconds.

Conclusions:

  • Surface-active proteins provide dynamic stabilization to coacervates via transient interface interactions.
  • This approach yields stable, dynamically exchanging synthetic condensate systems.
  • The findings advance understanding of membraneless organelle stability mechanisms.