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Reentrant liquid-liquid phase separation in protein solutions at elevated hydrostatic pressures.

Johannes Möller1, Sebastian Grobelny2, Julian Schulze1

  • 1Fakultät Physik/DELTA, TU Dortmund, 44221 Dortmund, Germany.

Physical Review Letters
|February 4, 2014
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Summary

High pressure induces reentrant liquid-liquid phase separation in dense lysozyme solutions. This phenomenon arises from pressure-dependent, solvent-mediated protein-protein interactions, revealing new insights into protein phase behavior under extreme conditions.

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Area of Science:

  • Biophysics
  • Soft Matter Physics
  • Protein Crystallography

Background:

  • Understanding protein phase behavior is crucial for biochemistry and drug formulation.
  • Dense protein solutions exhibit complex phase diagrams, including liquid-liquid phase separation (LLPS).
  • The influence of external parameters like pressure on protein interactions and phase behavior is not fully understood.

Purpose of the Study:

  • To investigate the effect of high pressure on the phase behavior of dense lysozyme solutions.
  • To characterize the pressure and temperature dependence of protein-protein interactions within the liquid-liquid phase separation region.
  • To elucidate the role of solvent-mediated interactions in driving phase separation under pressure.

Main Methods:

  • Small-angle X-ray scattering (SAXS) was employed to probe structural changes.
  • Experiments were conducted on dense lysozyme solutions across a range of temperatures and pressures.
  • Analysis focused on identifying and characterizing the liquid-liquid phase separation region.

Main Results:

  • A reentrant liquid-liquid phase separation region was discovered at elevated pressures.
  • The study identified a pressure dependence in the solvent-mediated protein-protein interactions.
  • These pressure-dependent interactions were found to be the origin of the observed reentrant phase behavior.

Conclusions:

  • High pressure can significantly alter the phase behavior of protein solutions.
  • Solvent-mediated interactions play a critical role in protein self-assembly and phase separation.
  • The findings provide a deeper understanding of protein interactions under non-physiological conditions, relevant for biophysics and materials science.