To gain further insight into the protein-binding mecha- nism we followed the time course of binding after bringing a dilute protein solution in contact with the polymers. Figure 4
(and FigureS9) shows that protein binding in all cases reached an equilibrium within 200 minutes, but the kinetics depended on both the protein and the adsorbent. First considering protein binding to the NIPs, HSA here exhibited a slower adsorption rate than IgG, which is consistent with the known adsorption kinetics of these two proteins to both hydrophilic and hydrophobic surfaces.[7,13] For the MIPs however, HSA displayed a faster adsorption, whereas IgG adsorbed more slowly than on the NIPs.
To gain further insight into the protein-binding mecha- nism we followed the time course of binding after bringing a dilute protein solution in contact with the polymers. Figure 4(and FigureS9) shows that protein binding in all cases reached an equilibrium within 200 minutes, but the kinetics depended on both the protein and the adsorbent. First considering protein binding to the NIPs, HSA here exhibited a slower adsorption rate than IgG, which is consistent with the known adsorption kinetics of these two proteins to both hydrophilic and hydrophobic surfaces.[7,13] For the MIPs however, HSA displayed a faster adsorption, whereas IgG adsorbed more slowly than on the NIPs.
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