Surface imprinting of pepsin via miniemulsion polymerization

Abstract

Surface imprinted polymers allow accessibility of the selective binding sites to large molecules such as proteins. In this work, small polymer particles offering a large surface area were prepared via miniemulsion polymerization in the presence of pepsin serving as a template molecule. The influence of four different functional monomers and of the amount of the template on the imprinting effect of pepsin was investigated. After the miniemulsion polymerization and a washing step, stable polymer suspensions with an average particle diameter of 400-600 nm and a specific surface area of 30-65 m² g^-1 were obtained. The results of detailed rebinding experiments revealed that the highest imprinting effect was achieved with (3-acrylamidopropyl)trimethylammonium chloride as a functional monomer and a high amount of the template. These polymer particles also showed selectivity for pepsin against various proteins. This approach provides a fundamental step towards the development of synthetic protein receptors and protein scavenger materials useful in biomimetic assays and for clean-up in biotechnology.