Immobilization of proteins on surfaces has drawn particular attention recently due to its importance in many nano-biotechnological applications such as proteomics, biosensors, or tissue engineering. Enzymatic approaches have advantages compared to other methods since such immobilization can be achieved covalently and site-specifically in mild conditions.We have used the transpeptidase sortase A to site-specifically bind recombinant fluorescent proteins (eGFP/RFP) to a functionalized gold surface and characterized these surfaces by fluorescence and atomic force microscopy.  We have also patterned eGFP on functionalized glass by microcontact printing. As the next step toward creating well-defined �molecular print-boards,� we made protein wires using a bifunctional eGFP with a genetically encoded peptidic protecting group enabling sequential deprotection-ligation steps and thus cyclic deposition of monomeric units in a manner analogous to other solid-phase synthesis applications such as peptide or oligonucleotide synthesis. Thus, layer-by-layer assembly of surface-attached, oriented molecular wires can be accomplished in a controlled manner.

Generating 2D and 3D protein assemblies using Sortase A

245th National Meeting (2013)

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