Water Molecule Structure on Material Interface Related to Protein Adsorption

Abstract

Adsorbed proteins initiate the undesirable phenomena like blood coagulation and immune response, and lead to the negative effects on human body and function of biodevices. Thus, the suppression of protein adsorption is essential property for biomaterials. Therefore, interfacial water molecules may play a key role on protein adsorption. In this study, various types of surface ; hydrophobic, hydrophilic, anionic, cationic and zeitterionic were prepared by high-density polymer brush having different molecular structure. The amount of adsorbed negatively and positively charged protein was analyzed by quartz crystal microbalance (QCM) method to investigate the protein adsorption on polymer brush surfaces quantitatively. Structure of interfacial water at the interface between polymer brush and water media was investigated using sum-frequency generation (SFG) spectroscopy. From the quantitative comparison with protein adsorption and structure of interfacial water molecule of each polymer brush, it is concluded that the interfacial water molecules, which form strong hydrogen bonding is a strong relation to the suppression of protein adsorption.