| Abstract
| - Derivatized polymer brushes grafted throughout the pores of an alumina support can adsorb as much as 150 mg of protein/cm3 of membrane. Nine cycles of protein loading, elution, and membrane regeneration resulted in no detectable loss of binding capacity.
- The use of atom transfer radical polymerization to grow poly(2-hydroxyethyl methacrylate) (PHEMA)brushes in porous alumina followed by functionalization of the PHEMA with nitrilotriacetate−Cu2+complexes yields membranes that adsorb proteins via coordination of Cu2+ to histidine residues. Adsorptionisotherms show that these membranes have binding capacities as high as 0.9 mg of bovine serum albumin(BSA)/cm2 of external membrane surface area (150 mg/cm3 of membrane), and breakthrough curvesindicate that saturation of the membranes with BSA or myoglobin occurs in less than 15 min. The efficiencyof protein elution with ethylenediaminetetraacetic acid (EDTA) solutions is essentially 100%, and themembranes show no detectable decrease in capacity over nine cycles of binding, elution, and regenerationwith Cu2+. The unusually high capacity of these membranes for rapid protein binding makes them attractivefor applications such as purification of His-tag proteins.
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