title: Immobilization of Ferrocene-Modified SNAP-Fusion Proteins.
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.
authors: Molecular NanoFabrication Group, MESA+ Institute for Nanotechnology, University of Twente, P.O. Box 217, 7500 AE, Enschede, The Netherlands. p.jonkheijm@utwente.nl.
authors: Dorothee
authors: D
authors: Wasserberg
authors: Dana A
authors: DA
authors: Uhlenheuer
authors: Pauline
authors: P
authors: Neirynck
authors: Jordi
authors: J
authors: Cabanas-Danés
authors: Jan Hendrik
authors: JH
authors: Schenkel
authors: Bart Jan
authors: BJ
authors: Ravoo
authors: Qi
authors: Q
authors: An
authors: Jurriaan
authors: J
authors: Huskens
authors: Lech-Gustav
authors: LG
authors: Milroy
authors: Luc
authors: L
authors: Brunsveld
authors: Pascal
authors: P
authors: Jonkheijm