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Open AccessArticle

Immobilization of Ferrocene-Modified SNAP-Fusion Proteins

Molecular NanoFabrication Group, MESA+ Institute for Nanotechnology, University of Twente, P.O. Box 217, 7500 AE, Enschede, The Netherlands
Laboratory of Chemical Biology, Department of Biomedical Engineering, Eindhoven University of Technology, P.O. Box 513, 5600 MB, Eindhoven, The Netherlands
Institute of Organic Chemistry, Westfaelische Wilhelms-Universität Muenster, Corrensstrasse 40, 48149 Münster, Germany
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2013, 14(2), 4066-4080;
Received: 30 November 2012 / Revised: 4 February 2013 / Accepted: 4 February 2013 / Published: 18 February 2013
(This article belongs to the Special Issue Molecular Self-Assembly 2012)
PDF [606 KB, uploaded 19 June 2014]


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. View Full-Text
Keywords: host-guest chemistry; protein immobilization; protein modifications; cyclodextrin; cucurbituril; ferrocene host-guest chemistry; protein immobilization; protein modifications; cyclodextrin; cucurbituril; ferrocene

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This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Wasserberg, D.; Uhlenheuer, D.A.; Neirynck, P.; Cabanas-Danés, J.; Schenkel, J.H.; Ravoo, B.J.; An, Q.; Huskens, J.; Milroy, L.-G.; Brunsveld, L.; Jonkheijm, P. Immobilization of Ferrocene-Modified SNAP-Fusion Proteins. Int. J. Mol. Sci. 2013, 14, 4066-4080.

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