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

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


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzymes, Immobilized / chemistry*
  • Enzymes, Immobilized / metabolism
  • Guanidines / chemistry*
  • O(6)-Methylguanine-DNA Methyltransferase / chemistry*
  • O(6)-Methylguanine-DNA Methyltransferase / metabolism
  • Printing*
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism
  • Substrate Specificity
  • Surface Properties


  • Enzymes, Immobilized
  • Guanidines
  • Recombinant Fusion Proteins
  • O(6)-Methylguanine-DNA Methyltransferase