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Supramolecular Assays for Mapping Enzyme Activity by Displacement‐Triggered Change in Hyperpolarized 129 Xe Magnetization Transfer NMR Spectroscopy
Author(s) -
Schnurr Matthias,
SloniecMyszk Jagoda,
Döpfert Jörg,
Schröder Leif,
Hennig Andreas
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201507002
Subject(s) - magnetization transfer , chemistry , nuclear magnetic resonance spectroscopy , magnetization , supramolecular chemistry , spectroscopy , nuclear magnetic resonance , biosensor , analytical chemistry (journal) , molecule , stereochemistry , magnetic resonance imaging , organic chemistry , biochemistry , physics , medicine , quantum mechanics , magnetic field , radiology
Reversibly bound Xe is a sensitive NMR and MRI reporter with its resonance frequency being influenced by the chemical environment of the host. Molecular imaging of enzyme activity presents a promising approach for disease identification, but current Xe biosensing concepts are limited since substrate conversion typically has little impact on the chemical shift of Xe inside tailored cavities. Herein, we exploit the ability of the product of the enzymatic reaction to bind itself to the macrocyclic hosts CB6 and CB7 and thereby displace Xe. We demonstrate the suitability of this method to map areas of enzyme activity through changes in magnetization transfer with hyperpolarized Xe under different saturation scenarios.