Protein Dimerization Induced by Supramolecular Interactions with Cucurbit[8]uril

Hosted dimerization: Proteins such as yellow fluorescent protein (YFP) with an N‐terminal FGG peptide motif form dimers mediated by supramolecular interactions with cucurbit[8]uril (see scheme). The protein dimerization, which is observed by FRET and size‐exclusion chromatography, can be reversed wi...

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Veröffentlicht in:	Angewandte Chemie (International ed.) 2010-01, Vol.49 (5), p.895-898
Hauptverfasser:	Nguyen, Hoang D, Dang, Dung T, van Dongen, Joost L.J, Brunsveld, Luc
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacterial Proteins - chemistry Chromatography, Gel cucurbituril Fluorescence Resonance Energy Transfer Green Fluorescent Proteins - chemistry host-guest chemistry Luminescent Proteins - chemistry Macrocyclic Compounds - chemistry Paraquat - chemistry peptide recognition protein dimerization Protein Interaction Domains and Motifs Protein Multimerization supramolecular chemistry
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Beschreibung
Zusammenfassung:	Hosted dimerization: Proteins such as yellow fluorescent protein (YFP) with an N‐terminal FGG peptide motif form dimers mediated by supramolecular interactions with cucurbit[8]uril (see scheme). The protein dimerization, which is observed by FRET and size‐exclusion chromatography, can be reversed with methyl viologen as a bioorthogonal ligand, which displaces the FGG motifs from the cucurbit[8]uril host.
ISSN:	1433-7851 1521-3773
DOI:	10.1002/anie.200904413