Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 18, Issue 22, Pages 6788-6794Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201200238
Keywords
cyclodextrin; host-guest systems; immobilization; protein modifications; vesicles
Categories
Funding
- ERC [204554, 259183]
- DAAD [D/08/46093]
- Alexander von Humboldt Foundation
- DFG [Ra-1731/1-2]
- Dutch Ministry of Economic Affairs, Agriculture and Innovation
- European Research Council (ERC) [259183, 204554] Funding Source: European Research Council (ERC)
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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 hostguest 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.
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