We thank Peter Schmieder for helpful discussions, Bernhard Schmikale for synthesizing cage-coupled HA peptide, and Werner Hoffmann and Karl-Heinz Rhein for probe coil design. This work was supported by grant 01GU0514 of the BMBF to C.F., K.F., and O.R. MHC=major histocompatibility complex.
Communication
A Xenon-129 Biosensor for Monitoring MHC–Peptide Interactions†
Article first published online: 30 APR 2009
DOI: 10.1002/anie.200806149
Copyright © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Schlundt, A., Kilian, W., Beyermann, M., Sticht, J., Günther, S., Höpner, S., Falk, K., Roetzschke, O., Mitschang, L. and Freund, C. (2009), A Xenon-129 Biosensor for Monitoring MHC–Peptide Interactions. Angewandte Chemie International Edition, 48: 4142–4145. doi: 10.1002/anie.200806149
- †
Publication History
- Issue published online: 19 MAY 2009
- Article first published online: 30 APR 2009
- Manuscript Revised: 12 MAR 2009
- Manuscript Received: 17 DEC 2008
Funded by
- BMBF
Keywords:
- antigens;
- biosensors;
- NMR spectroscopy;
- peptides;
- xenon
Graphical Abstract

Caged in: The formation of a complex between a peptide ligand and a major histocompatibility complex (MHC) class II protein is detected by a 129Xe biosensor. Cryptophane molecules that trap Xe atoms are modified with a hemagglutinin (HA) peptide, which binds to the MHC protein. The interaction can be monitored by an NMR chemical shift change of cage–HA bound 129Xe.
Abstract
Caged in: The formation of a complex between a peptide ligand and a major histocompatibility complex (MHC) class II protein is detected by a 129Xe biosensor. Cryptophane molecules that trap Xe atoms are modified with a hemagglutinin (HA) peptide, which binds to the MHC protein. The interaction can be monitored by an NMR chemical shift change of cage–HA bound 129Xe.

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