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    Benzylguanine Thiol Self-Assembled Monolayers for the Immobilization of SNAP-tag Proteins on Microcontact-Printed Surface Structures

    Year: 2010

    Journal: Langmuir, 2010, 26 (9), pp 6097–6101, 20100827

    Authors: Engin S. †, Trouillet V. ‡, Franz C.M. †, Welle A. §, Bruns M. ‡, Wedlich D. *†

    Last authors: Doris Wedlich

    Organizations: † Center for Functional Nanostructures ‡ Institute for Materials Research III § Institute for Biological Interfaces Karlsruhe Institute for Technology (KIT), Kaiserstrasse 12, D-76131 Karlsruhe, Germany

    Country: Germany

    The site-selective, oriented, covalent immobilization of proteins on surfaces is an important issue in the establishment of microarrays, biosensors, biocatalysts, and cell assays. Here we describe the preparation of self-assembled monolayers consisting of benzylguanine thiols (BGT) to which SNAP-tag fusion proteins can be covalently linked. The SNAP-tag, a modified O6-alkylguanine-DNA alkyltransferase (AGT), reacts with the headgroup of BGT and becomes covalently bound upon the release of guanine. Bacterially produced recombinant His-tag-SNAP-tag-GFP was used to demonstrate the site-specific immobilization on BGT surface patterns created by microcontact printing (μCP). With this versatile method, any SNAP-tag protein can be coupled to a surface.