During the past two decades, there was an exponential increase of research for molecularly imprinted materials. It started from ions to small molecules over peptides and finally reached macromolecules and proteins, viruses, DNA and cells. The field of protein imprinting and recognition is just about to be further investigated and developed. This work describes the challenging task of the development of tailor-made molecularly non-imprinted (NIP) and imprinted (MIP) polymers in two versions: hydrogels and nanoparticles. In contrast to literature, within this thesis, specially designed and synthesized monomers are used to create a specific polymer for a certain target. With the help of the amino acid complementary monomers, this work enables a design of highly specific and selective polymers which can, e. g., block protein or enzymatic functions, hinder protein-protein interactions or act like synthetic antibodies. The high affinity of the bisphosphonate-monomer could already be demonstrated by the work of Ertürk, Akhoundian, Lueg-Althoff et al. in imprinted biosensors for trypsin with a detection limit below picomolar (pM) concentrations. Monomers and (non-)imprinted polymers: In this thesis two approaches are presented. On the one hand, an optimization of a key functional monomer is described as well as new monomers are added to the library of functional monomers. On the other hand, new polymer material in the form of functionalized hydrogels are created by an innovative water-based synthesis. The usage of new and tailor-made functional monomers delivers slightly crosslinked polymers with special binding-sites. Moreover, it was possible to incorporate amino acid complementary monomers into polymer nanoparticles from the Shea approach. Characterization and analytics: Within the scope of this thesis, the polymeric materials are thoroughly characterized and analyzed by physicochemical examinations and other analytics. The development of a new assay for the determination of binding is the main challenge and task to overcome. Rebinding studies via fluorescent titrations offer a new way of analyzing these special protein-imprinted hydrogelic polymers.