title: Solvent effect on protein binding by polymer brush grafted onto porous membranes.
abstract: An epoxy-group-containing polymer chain was grafted onto the hollow-fiber form of a porous polyethylene membrane by the immersion of the electron beam-irradiated trunk polymer in glycidyl methacrylate diluted with methanol and 1-butanol. The epoxy group density ranged from 8.5 to 13.4 mol per kg of the trunk polymer. Subsequently, the epoxy groups produced were converted into sulfonic acid and diethylamino groups. The density of -SOH and -N(C2H5), groups was 0.40 and 2.2 mol per kg of the product. respectively. The polymer brush, defined as a polymer chain extending from the surface of a pore toward the interior of the pore, was evaluated from the determination of an equilibrium binding capacity of hen egg lysozyme (HEL) and bovine serum albumin (BSA). The polymer brush prepared in 1-butanol was found to be longer than that prepared in methanol from the determinations of liquid permeability and protein adsorptivity. The proteins were bound to the polymer brush prepared in 1-butanol, followed by the functionalization, at higher degrees of multilayer binding: about 30 for HEL and 6 for BSA.
authors.affiliation: Department of Materials Technology, Faculty of Engineering, Chiba University, Inage, Japan.
authors.forename: Daisuke
authors.initials: D
authors.lastname: Okamura
authors.forename: Kyoichi
authors.initials: K
authors.lastname: Sait
authors.forename: Kazuyuki
authors.initials: K
authors.lastname: Sugita
authors.forename: Masao
authors.initials: M
authors.lastname: Tamada
authors.forename: Takanobu
authors.initials: T
authors.lastname: Sugo
mesh_terms: D008567:Membranes, Artificial; D009113:Muramidase / Q000737:chemistry / Q000378:metabolism*; D011108:Polymers / Q000737:chemistry*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013499:Surface Properties
chemical_list: D008567:Membranes, Artificial; D011108:Polymers; D012710:Serum Albumin, Bovine; D009113:Muramidase