A cryptophane-based "turn-on" 129 Xe NMR biosensor for monitoring calmodulin

A cryptophane-based "turn-on" 129 Xe NMR biosensor for monitoring calmodulin

We present the first cryptophane-based "turn-on" Xe NMR biosensor, employing a peptide-functionalized cryptophane to monitor the activation of calmodulin (CaM) protein in solution. In the absence of CaM binding, interaction between the peptide and cryptophane completely suppresses the hype...

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Veröffentlicht in:Organic & biomolecular chemistry 2017-10, Vol.15 (42), p.8883-8887
Hauptverfasser: Riggle, Brittany A, Greenberg, Mara L, Wang, Yanfei, Wissner, Rebecca F, Zemerov, Serge D, Petersson, E James, Dmochowski, Ivan J
Format: Artikel
Sprache:eng
Schlagworte:
Biosensing Techniques
Calmodulin - analysis
Magnetic Resonance Spectroscopy
Models, Molecular
Polycyclic Compounds - chemistry
Xenon Isotopes
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Zusammenfassung:We present the first cryptophane-based "turn-on" Xe NMR biosensor, employing a peptide-functionalized cryptophane to monitor the activation of calmodulin (CaM) protein in solution. In the absence of CaM binding, interaction between the peptide and cryptophane completely suppresses the hyperpolarized Xe-cryptophane NMR signal. Biosensor binding to Ca -activated CaM produces the expected Xe-cryptophane NMR signal.
ISSN:1477-0520
1477-0539
DOI:10.1039/C7OB02391J