An easy preparation of ‘monolithic type’ hydrophilic solid phase: Capability for affinity resin to isolate target proteins

• Published in: Bioorganic & medicinal chemistry Vol. 14; no. 16; pp. 5549 - 5554
• Main Authors: Mori, Tomoko, Takahashi, Teruki, Shiyama, Takaaki, Tanaka, Akito, Hira, Natsuki, Tanaka, Nobuo, Hosoya, Ken
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 15.08.2006; Elsevier Science
• Subjects: Adsorption; Affinity resins; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Blotting, Western; Calcineurin - isolation & purification; Chromatography, Affinity - methods; Cross-Linking Reagents - chemistry; Ethylene Glycols - chemistry; FK506; Fundamental and applied biological sciences. Psychology; General aspects, investigation methods; Medical sciences; Miscellaneous; Monolith; Pharmacology. Drug treatments; Poly(methacrylate); Proteins; Proteins - chemistry; Proteins - isolation & purification; Resins, Synthetic - chemistry; Solvents - chemistry; Tacrolimus - chemistry; Affinity resins; FK506; Poly(methacrylate); Monolith; Methacrylate polymer; Ligand; Immobilization; Lactone; Crosslink agent; Macrolide; Hydrophily; Ethylene oxide polymer; Immunomodulator; Binding protein; Adsorption; Tacrolimus; Affinity; Immunosuppressive agent; Solid phase; Physicochemical properties
• ISSN: 0968-0896; 1464-3391
• DOI: 10.1016/j.bmc.2006.04.028

An easy preparation method of monolithic type hydrophilic solid phase was discussed. Newly invented functional monomer with a hydrophilic cross-linking agent was co-polymerized to realize well-controlled monolithic co-continuous structure by use of diethylene glycol as porogenic solvent. We were able to control the content of the functional monomer up to 40 vol% without loss of monolithic structure. Those prepared were utilized as affinity resins after immobilization of FK506, an immunosuppressive drug as a ligand. It was found that the affinity resins prepared were hydrophilic enough to eliminate non-specific adsorption of proteins, while two of the target proteins of FK506 tested were successfully captured.