How the dynamics of subsurface hydration regulates protein-surface interactions.

The role of water structure near surfaces has been scrutinized extensively because it is accepted to control protein-surface interactions, however, often avoiding effects of hydration dynamics. Relating to this, we have recently discussed how the amount and state of water, accumulated within various hydrophobic-to-hydrophilic subsurface gradients of plasma polymer films, influence the magnitude of adsorbed bovine serum albumin, spurring the hypothesis of the presence of a subsurface dipolar field. This study now analyzes the kinetics of hydration by systematically introducing modified gradient architectures and relating different hydration times to the adsorption of a dipolar probing protein. We find that dry-stored subsurface gradients, owing nominally identical surface characteristics, exhibits comparable surface potential and protein adsorption values, while they behave in a different manner at transient hydration times of few hours, before reaching near-equilibrium state of the hydration. A characteristic hydration time is found where protein adsorption on gradient films is minimal, unveiling the transient nature of the effect. In general, protein adsorption is sensitive to the time allowed for hydration of the adsorbent surface, supporting our initial hypothesis inasmuch as the quantity as well as quality of water inside the subsurface matrix is crucial for controlling protein-surface interactions.