Abstract: A novel method for a surface protein imprinting through a reactive "reading" of protein surface structure is described. First, protein molecules are chemically bound to a reactive ultrathin polymer layer. Next, the anchored proteins are removed by protease treatment. Residual amino acids become grafted to the surface and imitate the surface chemistry of the template molecule. However, the simple imprinting without additional template shape recognition does not show reproducible selectivity of the imprints. A further development of the approach is the deposition of an unsaturated protein monolayer and filling the space surrounding the adsorbed biomolecules with grafted poly(ethylene glycol) (PEG) layer. This leads to formation of islands of spatial pockets for the template with complementary chemistry at the bottom, embedded into a PEG layer with low non-specific protein adsorption capabilities.
Template and target information: protein