Supramolecular Assays for Mapping Enzyme Activity by Displacement-Triggered Change in Hyperpolarized 129Xe Magnetization Transfer NMR Spectroscopy
Dr. Matthias Schnurr
ERC Project BiosensorImaging, Leibniz-Institut für Molekulare Pharmakologie (FMP), Campus BerlinBuch, Robert-Rössle-Strasse 10, 13125 Berlin (Germany)
These authors contributed equally to this work.
Search for more papers by this authorDipl.-Chem. Jagoda Sloniec-Myszk
BAM Bundesanstalt für Materialforschung und -prüfung, Richard-Willstätter-Strasse 11, 12489 Berlin (Germany)
These authors contributed equally to this work.
Search for more papers by this authorDr. Jörg Döpfert
ERC Project BiosensorImaging, Leibniz-Institut für Molekulare Pharmakologie (FMP), Campus BerlinBuch, Robert-Rössle-Strasse 10, 13125 Berlin (Germany)
Search for more papers by this authorCorresponding Author
Dr. Leif Schröder
ERC Project BiosensorImaging, Leibniz-Institut für Molekulare Pharmakologie (FMP), Campus BerlinBuch, Robert-Rössle-Strasse 10, 13125 Berlin (Germany)
Leif Schröder, ERC Project BiosensorImaging, Leibniz-Institut für Molekulare Pharmakologie (FMP), Campus BerlinBuch, Robert-Rössle-Strasse 10, 13125 Berlin (Germany)
Andreas Hennig, Department of Life Sciences and Chemistry, Jacobs University Bremen, Campus Ring 1, 28759 Bremen (Germany)
Search for more papers by this authorCorresponding Author
Dr. Andreas Hennig
Department of Life Sciences and Chemistry, Jacobs University Bremen, Campus Ring 1, 28759 Bremen (Germany)
These authors contributed equally to this work.
Leif Schröder, ERC Project BiosensorImaging, Leibniz-Institut für Molekulare Pharmakologie (FMP), Campus BerlinBuch, Robert-Rössle-Strasse 10, 13125 Berlin (Germany)
Andreas Hennig, Department of Life Sciences and Chemistry, Jacobs University Bremen, Campus Ring 1, 28759 Bremen (Germany)
Search for more papers by this authorDr. Matthias Schnurr
ERC Project BiosensorImaging, Leibniz-Institut für Molekulare Pharmakologie (FMP), Campus BerlinBuch, Robert-Rössle-Strasse 10, 13125 Berlin (Germany)
These authors contributed equally to this work.
Search for more papers by this authorDipl.-Chem. Jagoda Sloniec-Myszk
BAM Bundesanstalt für Materialforschung und -prüfung, Richard-Willstätter-Strasse 11, 12489 Berlin (Germany)
These authors contributed equally to this work.
Search for more papers by this authorDr. Jörg Döpfert
ERC Project BiosensorImaging, Leibniz-Institut für Molekulare Pharmakologie (FMP), Campus BerlinBuch, Robert-Rössle-Strasse 10, 13125 Berlin (Germany)
Search for more papers by this authorCorresponding Author
Dr. Leif Schröder
ERC Project BiosensorImaging, Leibniz-Institut für Molekulare Pharmakologie (FMP), Campus BerlinBuch, Robert-Rössle-Strasse 10, 13125 Berlin (Germany)
Leif Schröder, ERC Project BiosensorImaging, Leibniz-Institut für Molekulare Pharmakologie (FMP), Campus BerlinBuch, Robert-Rössle-Strasse 10, 13125 Berlin (Germany)
Andreas Hennig, Department of Life Sciences and Chemistry, Jacobs University Bremen, Campus Ring 1, 28759 Bremen (Germany)
Search for more papers by this authorCorresponding Author
Dr. Andreas Hennig
Department of Life Sciences and Chemistry, Jacobs University Bremen, Campus Ring 1, 28759 Bremen (Germany)
These authors contributed equally to this work.
Leif Schröder, ERC Project BiosensorImaging, Leibniz-Institut für Molekulare Pharmakologie (FMP), Campus BerlinBuch, Robert-Rössle-Strasse 10, 13125 Berlin (Germany)
Andreas Hennig, Department of Life Sciences and Chemistry, Jacobs University Bremen, Campus Ring 1, 28759 Bremen (Germany)
Search for more papers by this authorGraphical Abstract
The supramolecular recognition properties of cucurbiturils are exploited in a modified signal-transfer approach in Xe NMR spectroscopy. Magnetic resonance imaging of enzymatic reactions was possible in this way by displacement of hyperpolarized 129Xe.
Abstract
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.
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