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

We present the first cryptophane-based "turn-on" 129 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...

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Bibliographic Details
Published in:Organic & biomolecular chemistry 2017-10, Vol.15 (42), p.8883-8887
Main Authors: Riggle, Brittany A, Greenberg, Mara L, Wang, Yanfei, Wissner, Rebecca F, Zemerov, Serge D, Petersson, E. James, Dmochowski, Ivan J
Format: Article
Language:English
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Summary:We present the first cryptophane-based "turn-on" 129 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 129 Xe-cryptophane NMR signal. Biosensor binding to Ca 2+ -activated CaM produces the expected 129 Xe-cryptophane NMR signal. A cryptophane-peptide conjugate identifies activated calmodulin in solution, with appearance of Xe-129 NMR signal.
ISSN:1477-0520
1477-0539
DOI:10.1039/c7ob02391j