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Clickable Antifouling Polymer Brushes for Polymer Pen Lithography

Clickable Antifouling Polymer Brushes for Polymer Pen Lithography

U. Bog, A. de los Santos Pereira, S. L. Mueller, S. Havenridge, V. Parrillo, M. Bruns, A. E. Holmes, C. Rodriguez-Emmenegger, H. Fuchs, M. Hirtz


ACS Appl. Mater. Interfaces 9 (2017) 12109-12117

Date: 2017

Protein-repellent reactive surfaces that promote localized specific binding are highly desirable for applications in the biomedical field. Nonspecific adhesion will compromise the function of bioactive surfaces, leading to ambiguous results of binding assays and negating the binding specificity of patterned cell-adhesive motives. Localized specific binding is often achieved by attaching a linker to the surface and the other side of the linker is used to bind specifically to a desired functional agent, as e.g. proteins, antibodies, fluorophores, depending on the function required by the application. We present a protein-repellent polymer brush enabling highly specific covalent surface immobilization of biorecognition elements by strain-promoted alkyne-azide cycloaddition click chemistry for selective protein adhesion. The protein-repellent polymer brush is functionalized by highly localized molecular binding sites in the low micron range using polymer pen lithography (PPL). Due to the massive parallelization of writing pens, the tunable PPL printed patterns can span over square centimeter areas. The selective binding of the protein streptavidin to these surface sites is demonstrated while the remaining polymer brush surface is resisting non-specific adsorption without any prior blocking by bovine serum albumin (BSA). In contrast to the widely used BSA blocking, the reactive polymer brushes are able to significantly reduce non-specific protein adsorption, which is the cause of biofouling. This was achieved for solutions of single proteins as well as complex biological fluids. The remarkable fouling resistance of the polymer brushes has the potential to improve the multiplexing capabilities of protein probes and therefore impact biomedical research and applications.