Journal
LANGMUIR
Volume 26, Issue 9, Pages 6097-6101Publisher
AMER CHEMICAL SOC
DOI: 10.1021/la904829y
Keywords
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Funding
- German Research Foundation (DFG)
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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 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 (mu CP). With this versatile method, any SNAP-tag protein can be coupled to a surface.
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