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Updated: Sep 22, 2025
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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
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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
1Fakultät Physik/DELTA, TU Dortmund, 44221 Dortmund, Germany.
The Journal of Physical Chemistry. B
|May 20, 2022
Summary
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.
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.
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