A new approach, combining metal-coordination with molecular imprinting technology, was developed to prepare protein-affinity materials, which showed higher specific recognition ability towards the target protein than those prepared using either metal-coordination or molecular imprinting technology.Isolation and detection of target biomolecules, such as biomarkers from complex samples, are of great significance in life science research.1 Although high-performance liquid chromatography and capillary electrophoresis have shown great potential in the separation of complicated samples, immunoaffinity chromatography has been regarded as one of the most powerful methods to capture interested biomolecules selectively. However, the high cost, poor stability and difficult acquisition of antibodies might hinder the wide application of immunoaffinity chromatography. Therefore, it is highly desirable and useful to develop new affinity materials, to achieve the easy, fast, low-cost and high selective separation of target biomacromolecules. 2Immobilized metal ion affinity chromatography (IMAC) has been employed for the purification of proteins, peptides or His-tagged oligonucleotides, based on the different interactions between samples and metal ions immobilized on matrices.3 Thus, for proteins with similar affinity to metal ions, they can hardly be separated by IMAC.Molecular imprinting is considered as an elegant and convenient technology that can introduce specific recognition and binding sites in materials, which are geometrically and chemically complementary to the template. 4 Such created cavities can act as artificial recognition elements, and exhibit high selectivity toward the target molecules, including a large and diverse set of organic compounds and biomolecules. If we combine IMAC with molecular imprinting for biomacromolecule recognition, a new affinity material, with both metal ions having specific recognition cavity serving as recognition elements, could be prepared. Such an idea is quite different from the previous work, 6 in which metal ions chelated by functional monomers were positioned on the silica surface at precise distances to match the size of template protein. However without cross-linking, the linear polymer layer was brush-like, which might be too flexible to maintain stable cavities for template protein recognition.In this work, we have prepared a new kind of affinity materials for the specific recognition of porcine serum albumin (PSA) combining metal coordination with surface molecular imprinting. Herein, metal ions not only work as anchor points for the immobilization of PSA during the formation of crosslinked imprinted layer, enabling the facile removal of template after polymerization, but also serve as recognition elements for the rebinding of target proteins, together with imprinted cavities. Therefore, the selectivity of such materials should be improved than those prepared with the principle of either IMAC or molecular imprinting.The procedure for preparing surface protein-imprinted parti...

Polymer self-assembly was developed as an epitope imprinting strategy involving facile processes and high recognition site density. As a model, transferrin epitope imprinted polyethersulfone (PES) beads were successfully fabricated using this technique. The imprinted beads demonstrated excellent selectivity toward the transferrin epitope and transferrin even in the real sample.