Affinity monoliths generated by in situ polymerization of the ligand

An affinity monolith with a novel immobilization strategy was developed lea ding to a tailored pore structure. Hereby the ligand is conjugated to one o f the monomers of the polymerization mixture prior to polymerization. After the polymerization, a monolithic structure was obtained either ready to us e for affinity chromatography or ready for coupling of additional ligand to further increase the binding capacity. The model ligand, a peptide directe d against lysozyme, was conjugated to glycidyl methacrylate prior to the po lymerization. With this conjugate, glycidyl methacrylate, and ethylene dime thacrylate, a monolith was formed and tested with lysozyme. A better ligand presentation was achieved indicated by the higher affinity constant compar ed to a conventional sorbent.