Immobilization of ferrocene-modified SNAP-fusion proteins

D. Wasserberg, D. Uhlenheuer, P. Neirynck, Pauline Neirynck, Jordi Cabanas Danés, J.H. Schenkel, B.J. Ravoo, Q. An, Jurriaan Huskens, L.G. Milroy, Luc Brunsveld, Pascal Jonkheijm

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Abstract

The supramolecular assembly of proteins on surfaces has been investigated via the site-selective incorporation of a supramolecular moiety on proteins. To this end, fluorescent proteins have been site-selectively labeled with ferrocenes, as supramolecular guest moieties, via SNAP-tag technology. The assembly of guest-functionalized SNAP-fusion proteins on cyclodextrin- and cucurbit[7]uril-coated surfaces yielded stable monolayers. The binding of all ferrocene fusion proteins is specific as determined by surface plasmon resonance. Micropatterns of the fusion proteins, on patterned cyclodextrin and cucurbituril surfaces, have been visualized using fluorescence microscopy. The SNAP-fusion proteins were also immobilized on cyclodextrin vesicles. The supramolecular SNAP-tag labeling of proteins, thus, allows for the assembly of modified proteins via supramolecular host-guest interaction on different surfaces in a controlled manner. These findings extend the toolbox of fabricating supramolecular protein patterns on surfaces taking advantage of the high labeling efficiency of the SNAP-tag with versatile supramolecular moieties
Original languageEnglish
Pages (from-to)4066-4080
Number of pages15
JournalInternational journal of molecular sciences
Volume14
Issue number2
DOIs
Publication statusPublished - 2013

Keywords

  • METIS-301602
  • IR-90133

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