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


Sinem Engin , Vanessa Trouillet , Clemens M. Franz , Alexander Welle , Michael Bruns and Doris Wedlich



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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.

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Date added: 2012-08-17 13:17:10 | Last time updated: 2012-08-17 11:17:10 | Viewed: 1412 times

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