Peptide-crosslinked molecularly imprinted polymers for efficient separation of immunoglobulin G from human serum.

Low-cost and highly effective methods are highly desirable to replace the costly ethanol fractionation and affinity chromatography in IgG isolation from human plasma. Molecularly imprinted polymers (MIPs) of IgG are potential candidates, however, they still suffer from severe problems such as difficult template removal and low imprinting efficiency. Here, a recently developed strategy was adopted to overcome these problems. The MIPs were synthesized using poly(L-glutamic acid) (PLGA) peptide crosslinkers instead of commonly used crosslinkers, such as N , N -methylenebisacrylamide (BIS). Because of the pH-induced helix-coil transition and the precise folding of the peptide segments in the polymers, the imprint cavities can be enlarged by adjusting the pH from 5.0 to 7.0, but their original size and shape are restored when the pH is adjusted back. Therefore, the IgG template can be eluted completely under mild conditions, and significantly improved imprinting efficiency can be achieved. Compared with BIS-crosslinked MIP, 8.6 times more binding sites can be created by molecular imprinting PLGA-crosslinked MIP. The factors influencing the performance of the MIP were studied systematically. An optimized MIP with a high adsorption capacity (612.5 mg g -1 ), high IF (4.92), and high selectivity was obtained. The adsorption capacity and selectivity of the MIP are much higher than the previously reported IgG MIPs. Because of its high adsorption capacity and selectivity, it can separate IgG from human serum effectively, affording high purity products.