Clarification of Protein Adsorption at Polymer Brush Surfaces Based on Water Structure Surrounding the Surface

摘要

Protein adsorption behavior at the biocompatible polymer brush surfaces was quantitatively investigated based on the water structure surrounding the surface. The high repellency of protein adsorption at the polymer brush surface was analyzed using both quartz crystal microbalance with dissipation method and force-distance curve measurement in atomic force microscopy. The diffusion coefficients of water molecules among micro-silica beads with polymer brush layers were analyzed using nuclear magnetic resonance spectroscopy. These results clearly demonstrated that the dynamics of water molecules determine the protein adsorption behavior at the biocompatible polymer brush surfaces. Thus, polymer brush surface with water molecules with high diffusion coefficients, such as a zwitterionic group-bearing polymer brush surface, was effective in inhibiting protein adsorption.