Abstract
The adsorption of lysozyme protein was measured ex situ on well-characterized gold surfaces coated by end-tethered polyethylene oxide brushes of various molecular weights and controlled grafting densities. The adsorbed amount of protein for different molecular weight brushes was found to collapse onto one master curve when plotted against brush coverage. We interpret this relationship in terms of a model involving site-blocking of the adsorption of proteins at the substrate and discuss the role of the physical attraction of PEO segments to gold. We account for our observation of a simple exponential relationship between protein adsorption and normalized brush coverage with a simple protein adsorption model. In contrast to other studies in similar systems, we do not observe protein adsorption on brushes at high grafting density, and we suggest that this discrepancy may be due to the solubility effects of salt upon the brushes, influencing their protein binding affinity, in the limit of high grafting density and high brush volume fraction.
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