Affinity monoliths generated by in situ polymerization of the ligand.
An affinity monolith with a novel immobilization strategy was developed leading to a tailored pore structure. Hereby the ligand is conjugated to one of the monomers of the polymerization mixture prior to polymerization. After the polymerization, a monolithic structure was obtained either ready to use for affinity chromatography or ready for coupling of additional ligand to further increase the binding capacity. The model ligand, a peptide directed against lysozyme, was conjugated to glycidyl methacrylate prior to the polymerization. With this conjugate, glycidyl methacrylate, and ethylene dimethacrylate, a monolith was formed and tested with lysozyme. A better ligand presentation was achieved indicated by the higher affinity constant compared to a conventional sorbent.
Hahn
R
R
Institute for Applied Microbiology, University of Agricultural Sciences, Vienna, Austria.
Podgomik
A
A
Merhar
M
M
Schallaun
E
E
Jungbauer
A
A
D002846:Chromatography, Affinity / Q000379:methods*; D003432:Cross-Linking Reagents / Q000737:chemistry; D004852:Epoxy Compounds / Q000737:chemistry; D008024:Ligands; D008689:Methacrylates / Q000737:chemistry; D009113:Muramidase / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D011108:Polymers / Q000737:chemistry*
D003432:Cross-Linking Reagents; D004852:Epoxy Compounds; D008024:Ligands; D008689:Methacrylates; D010455:Peptides; D011108:Polymers; C004919:ethylene dimethacrylate; D009113:Muramidase; C007870:glycidyl methacrylate