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Langmuir. 2010 May 4;26(9):6097-101. doi: 10.1021/la904829y.

Benzylguanine thiol self-assembled monolayers for the immobilization of SNAP-tag proteins on microcontact-printed surface structures.

Author information

1
Center for Functional Nanostructures, Karlsruhe Institute for Technology, Kaiserstrasse 12, D-76131 Karlsruhe, Germany.

Abstract

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 O(6)-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 (microCP). With this versatile method, any SNAP-tag protein can be coupled to a surface.

PMID:
20369837
DOI:
10.1021/la904829y
[Indexed for MEDLINE]

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