Solvent effect on protein binding by polymer brush grafted onto porous membranes

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...

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Bibliographic Details
Published in:Journal of Chromatography A 2002-04, Vol.953 (1), p.101-109
Main Authors: Okamura, Daisuke, Saito, Kyoichi, Sugita, Kazuyuki, Tamada, Masao, Sugo, Takanobu
Format: Article
Language:English
Subjects:
Albumin
Analytical, structural and metabolic biochemistry
Applied sciences
Biological and medical sciences
Exact sciences and technology
Exchange resins and membranes
Forms of application and semi-finished materials
Fundamental and applied biological sciences. Psychology
General aspects, investigation methods
Lysozyme
Membranes, Artificial
Muramidase - chemistry
Muramidase - metabolism
Polymer industry, paints, wood
Polymers - chemistry
Protein Binding
Proteins
Serum Albumin, Bovine - chemistry
Serum Albumin, Bovine - metabolism
Surface Properties
Technology of polymers
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Summary: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 –SO 3H and –N(C 2H 5) 2 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.
ISSN:0021-9673
DOI:10.1016/S0021-9673(02)00105-X