The attachment of proteins to a surface in such a way that the protein remains functional, is a key issue in many biotechnological processes. Here, we describe the controlled attachment with respect to kinetics, thermodynamics and orientation of SAv (streptavidin) through an orthogonal linker to β-cyclodextrin selfassembled monolayers. Both a univalent and a bivalent linker are used for this process. The immobilization strategy with the bivalent linker allows the stepwise adsorption of SAv on to the surface, allowing heterofunctionalization of SAv and thus the build-up of more complex bionanostructures at the surface.

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