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Phase separation in solutions with specific and nonspecific interactions.

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Protein solutions can separate into distinct phases under stress. Even with complex formation, proteins with multiple interaction sites can aggregate and phase separate, impacting solution stability.

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Area of Science:

  • Biophysics
  • Physical Chemistry
  • Computational Biology

Background:

  • Protein solutions are generally stable under physiological conditions.
  • Stress can induce phase separation (demixing) into protein-rich and protein-poor regions.
  • Understanding these phase separation phenomena is crucial for protein stability and function.

Purpose of the Study:

  • To investigate the critical conditions for phase separation in protein solutions.
  • To model protein interactions using both isotropic and specific directional forces.
  • To explore the role of protein complex formation and aggregation on phase separation.

Main Methods:

  • Utilized a lattice-gas model for proteins.
  • Employed Monte Carlo simulations to calculate critical conditions.
  • Applied statistical associating fluid theory (SAFT).
  • Investigated model proteins with up to four interaction patches.

Main Results:

  • Phase separation is suppressed by protein complex formation, which passivates associating sites.
  • Proteins with three or more patches can form extended aggregates that phase separate.
  • This aggregation-driven phase separation can occur even without nonspecific interactions.
  • A unified view of critical behavior in fluids with anisotropic interactions was developed.

Conclusions:

  • Protein complexation can stabilize solutions against phase separation.
  • However, anisotropic interactions, particularly with multiple patches, can lead to aggregation and phase separation.
  • These findings provide insights into the thermodynamic stability of protein solutions under various conditions.