An all-aqueous route to polymer brush-modified membranes with remarkable permeabilites and protein capture rates

作者：Anuraj Nishotha; Bhattacharjee Somnath; Geiger James H; Baker Gregory L^*; Bruening Merlin L

来源：Journal of Membrane Science, 2012, 389: 117-125.

DOI：10.1016/j.memsci.2011.10.022

• Affinity membranes
• Protein purification
• Macroinitiator
• His-tagged protein
• Polymer brushes

Microporous membranes are attractive for protein purification because convection rapidly brings proteins to binding sites. However, the low binding capacity of such membranes limits their applications. This work reports a rapid, aqueous procedure to create highly permeable, polymer brush-modified membranes that bind large amounts of protein. The synthetic method includes a 10-min adsorption of a macroinitiator in a hydroxylated nylon membrane and a subsequent 5-min aqueous atom transfer radical polymerization of 2-(methacryloyloxy)ethyl succinate from the immobilized initiator to form poly(acid) brushes. This procedure likely leads to more swollen, less dense brushes than polymerization from silane initiators, and thus requires less polymer to achieve the same binding capacity. The hydraulic permeability of the poly(acid) membranes is 4-fold higher than that of similar membranes prepared by growing brushes from immobilized silane initiators. These brush-containing nylon membranes bind 120 mg/cm(3) of lysozyme using solution residence times as short as 35 ms, and when functionalized with nitrilotriacetate (NTA)-Ni2+ complexes, they capture 85 mg/cm(3) of histidine(6)-tagged (His-tagged) Ubiquitin. Additionally the NTA-Ni2+-functionalized membranes isolate His-tagged myo-inositol-1-phosphate synthase directly from cell extracts and show %26gt;90% recovery of His-tagged proteins.

• 出版日期2012-2-1