Immobilization of Ferrocene-Modified SNAP-Fusion Proteins
Autor: | Jurriaan Huskens, Luc Brunsveld, Dorothee Wasserberg, Jordi Cabanas-Danés, Jan Hendrik Schenkel, Pauline Neirynck, Bart Jan Ravoo, Dana A. Uhlenheuer, Lech-Gustav Milroy, Pascal Jonkheijm, Qi An |
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Přispěvatelé: | Macromolecular and Organic Chemistry, Chemical Biology, Faculty of Science and Technology, Molecular Nanofabrication |
Jazyk: | angličtina |
Rok vydání: | 2013 |
Předmět: |
Supramolecular chemistry
macromolecular substances 010402 general chemistry 01 natural sciences Catalysis Article Supramolecular assembly Inorganic Chemistry lcsh:Chemistry host-guest chemistry protein immobilization protein modifications cyclodextrin cucurbituril ferrocene Cucurbituril Moiety Physical and Theoretical Chemistry Surface plasmon resonance Host–guest chemistry Molecular Biology lcsh:QH301-705.5 Spectroscopy chemistry.chemical_classification Cyclodextrin 010405 organic chemistry Chemistry Organic Chemistry technology industry and agriculture General Medicine Fusion protein Combinatorial chemistry 0104 chemical sciences Computer Science Applications lcsh:Biology (General) lcsh:QD1-999 lipids (amino acids peptides and proteins) |
Zdroj: | International Journal of Molecular Sciences International Journal of Molecular Sciences, 14(2), 4066-4080. Multidisciplinary Digital Publishing Institute (MDPI) International Journal of Molecular Sciences, Vol 14, Iss 2, Pp 4066-4080 (2013) International Journal of Molecular Sciences; Volume 14; Issue 2; Pages: 4066-4080 International journal of molecular sciences, 14(2), 4066-4080. Multidisciplinary Digital Publishing Institute (MDPI) |
ISSN: | 1422-0067 1661-6596 |
Popis: | 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. |
Databáze: | OpenAIRE |
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