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Updated: Dec 26, 2025

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
How the dynamics of subsurface hydration regulates protein-surface interactions
Ezgi Bülbül1, Dirk Hegemann2, Thomas Geue3
1Laboratory for Advanced Fibers, Empa, Swiss Federal Laboratories for Materials Science and Technology, 9014, St. Gallen, Switzerland; Laboratory for Surface Science and Technology, Department of Materials, ETH Zurich, 8093, Zurich, Switzerland.
Surface hydration dynamics significantly impact protein adsorption. This study reveals a characteristic hydration time where protein binding is minimal, highlighting the crucial role of water
Area of Science:
- Surface Science
- Biophysics
- Materials Science
Background:
- Water structure near surfaces is critical for protein-surface interactions.
- Previous work highlighted the influence of water accumulation in subsurface gradients on protein adsorption.
- A hypothesis of a subsurface dipolar field controlling these interactions was proposed.
Purpose of the Study:
- To analyze the kinetics of hydration in modified gradient architectures.
- To relate different hydration times to the adsorption of a dipolar probing protein.
- To investigate the transient nature of hydration effects on protein adsorption.
Main Methods:
- Systematic introduction of modified gradient architectures in plasma polymer films.
- Analysis of hydration kinetics by varying hydration times.
- Measurement of surface potential and adsorption of a dipolar probing protein.
Main Results:
- Dry-stored gradients with similar surface characteristics showed comparable initial potential and protein adsorption.
- Transient hydration (few hours) revealed distinct behaviors before reaching near-equilibrium.
- A characteristic hydration time was identified where protein adsorption reached a minimum.
Conclusions:
- Protein adsorption is sensitive to the time allowed for surface hydration.
- The quantity and quality of subsurface water are crucial for controlling protein-surface interactions.
- The findings support the hypothesis of a subsurface dipolar field influencing these dynamics.
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