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Abstract: As artificial antibodies, protein-imprinted materials offer many advantages such as long-term storage stability, potential reusability, resistance to harsh environments and low cost. However, they suffer from obvious disadvantages, when whole proteins are used as templates. First, it is difficult to retain the native conformation of template proteins during the polymerization process. Second, it is unavailable to obtain pure proteins, especially low abundance proteins as the templates. Third, the relatively large imprinted sites are able to bind a range of smaller non-targets, resulting in reduced selectivity. Epitopes are the regions within the structures of globular proteins that can be classified as antigenic determinants. The epitope's structural specificity usually represents the entire protein. And, they can be easily obtained through artificial synthesis. Currently, as an alternative to the target protein, epitopes have been successfully employed as templates to fabricate the recognition sites for several proteins. Compared with protein templates, epitope templates are much more robust and stable during the imprinting process. Moreover, epitope templates could be obtained in large scale with low cost, even for the rare proteins. In this review, we critically and comprehensively survey recent advances and applications in epitope imprinting. The epitope imprinting techniques have been developed into several formats, epitope bulk imprinting, grafted epitope surface imprinting, constrained epitope surface imprinting and synergic epitope surface imprinting according to how the template is presented in the imprinted materials. For the epitope bulk imprinting, binding sites were formed throughout a bulk material. The grafted epitope surface imprinting is achieved by immobilizing epitope on the film or particle surface and then polymerizing with monomers and crosslinkers to form a state-of-the-art recognition sites on the polymer or silica surface. In the constrained epitope surface imprinting, the epitope is confined between the matrix support and the final polymer matrix. Then the matrix support is removed to expose the recognition sites, usually by simply peeling imprinted polymer from the matrix or dissolving the matrix. To improve the affinities and selectivity, additional affinities were integrated into the epitope imprinted surface, which results in the technique of synergic epitope surface imprinting. More recently, application of epitope-imprinted materials has also increased substantially with the rapid development of the life sciences, although they are not as widely used as whole protein molecule imprinting. These are demonstrated in the aspect of the peptide recognition, protein recognition and cell recognition. Finally, we summarized the remaining challenges arising from the intrinsic properties of epitope imprinting, and proposed its future development direction.
Template and target information: review - MIPs imprinted with epitopes