Abstract

The adsorption of BSA and fibrinogen onto plasma-polymerized di-(ethylene glycol) vinyl ether, allylamine, and maleic anhydride films were investigated in detail by surface plasmon resonance spectroscopy (SPR). The chemical properties of the plasma polymers were initially determined by the plasma deposition conditions during the generation procedure. The analysis of the chemical structure of the films and the refractive index of plasma polymers in aqueous solution was carried out using Fourier transform infrared spectroscopy and waveguide mode spectroscopy, respectively. Using water contact angle measurement, the surface wettability of plasma polymers was also characterized. These properties have a critical influence on the behavior of protein adsorption on the surface of the plasma polymers. Protein adsorption was found to depend not only on the types of functionalized groups, but also on the plasma polymer thickness since the protein molecules penetrate into the plasma polymer network bulk. According to the size of protein molecules in aqueous solution and the amount of adsorbed proteins observed by SPR, the conformational changes of proteins could be deduced.

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