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Gelation Dynamics upon Pressure-Induced Liquid-Liquid Phase Separation in a Water-Lysozyme Solution.

M Moron1, A Al-Masoodi2, C Lovato2

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This study reveals that pressure-induced liquid-liquid phase separation (LLPS) in protein solutions leads to gelation. Dynamics slow down as the system approaches the phase boundary, indicating a transition to a gel-like state.

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Area of Science:

  • Soft Matter Physics
  • Biophysics
  • Materials Science

Background:

  • Liquid-liquid phase separation (LLPS) is crucial for cellular organization and function.
  • Understanding the dynamics of protein solutions near phase boundaries is key to comprehending gelation processes.

Purpose of the Study:

  • To investigate the kinetics and dynamics of pressure-induced LLPS in a water-lysozyme solution.
  • To characterize the transition from a liquid to a gel state in protein solutions.

Main Methods:

  • X-ray photon correlation spectroscopy (XPCS) was employed to probe dynamics.
  • Scattering invariants and kinetic data were analyzed to understand phase separation and coarsening.
  • Analysis of g2 functions and diffusion exponents characterized the viscoelastic properties.

Main Results:

  • The water-lysozyme solution reached the phase boundary without arrest during pressure-induced LLPS.
  • Coarsening dynamics slowed with increased quench depth.
  • A two-step decay in g2 functions and linear aging (τ ∝ tw) indicated gelation.
  • Fast superdiffusive and slow subdiffusive motions were observed, characteristic of viscoelastic networks.

Conclusions:

  • The protein solution transitions to a gel state upon reaching the phase boundary.
  • Pressure-induced LLPS in this system is directly linked to the onset of viscoelastic relaxation and gel formation.