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Abstract: Proteins are amphoteric biopolymers with unevenly charged exterior surfaces. Taking this point fully into account could accomplish ingenious recognition systems for the biological macromolecues. Molecularly imprinted polymers (MIPs) are good tools to study the interactions between polymeric matrices and template molecules. Here different protein imprinted cryogels were prepared. Imprinting factors (IFs) were determined with bovine serum albumin (BSA) as the template. The IF of the polymeric cryogel made from only acrylamide (AM) and N,N'-methylenebisacrylamide (BisAM) is about 1.38. The introduction of charged monomers, either acrylic acid or diallylamine, would increase IFs obviously. One of the basic cryogels gave the maximum IF (about 2.0) of that type. As both acrylic acid and diallylamine were involved, IFs were further increased. An amphoteric cryogel with a suitable acid-base ratio gave a high IF of about 3.7. Whatever used alone or both, too many added acidic or basic monomers resulted in IF reduction. Taking full advantage of charged groups in MIPs could be a good way to manipulate protein-polymer interactions. © 2016 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2016, 133, 43851
Template and target information: protein, bovine serum albumin, BSA
Author keywords: biocompatibility, gels, proteins