Directed Supramolecular Surface Assembly of SNAP-tag Fusion Proteins

D.A. Uhlenheuer, D. Wasserberg, C. Haase, Hoang D. Nguyen, J.H. Schenkel, Jurriaan Huskens, B.J. Ravoo, Pascal Jonkheijm, Luc Brunsveld

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39 Citations (Scopus)


Supramolecular assembly of proteins on surfaces and vesicles was investigated by site-selective incorporation of a supramolecular guest element on proteins. Fluorescent proteins were site-selectively labeled with bisadamantane by SNAP-tag technology. The assembly of the bisadamantane functionalized SNAP-fusion proteins on cyclodextrin-coated surfaces yielded stable monolayers. The binding of the fusion proteins is specific and occurs with an affinity in the order of 106 M−1 as determined by surface plasmon resonance. Reversible micropatterns of the fusion proteins on micropatterned cyclodextrin surfaces were visualized by using fluorescence microscopy. Furthermore, the guest-functionalized proteins could be assembled out of solution specifically onto the surface of cyclodextrin vesicles. The SNAP-tag labeling of proteins thus allows for assembly of modified proteins through a host–guest interaction on different surfaces. This provides a new strategy in fabricating protein patterns on surfaces and takes advantage of the high labeling efficiency of the SNAP-tag with designed supramolecular elements
Original languageUndefined
Pages (from-to)6788-6794
Number of pages7
JournalChemistry : a European journal
Issue number22
Publication statusPublished - 2012


  • METIS-289517
  • IR-84737

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