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Study of molecular interactions with 13C DNP-NMR

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Bibliographic Details
Title:	Study of molecular interactions with ¹³C DNP-NMR
Authors:	Lerche, Mathilde H.¹ mathilde.lerche@albeda.dk, Meier, Sebastian², Jensen, Pernille R.¹, Baumann, Herbert³, Petersen, Bent O.², Karlsson, Magnus¹, Duus, Jens Ø.², Ardenkjær-Larsen, Jan H.⁴
Source:	Journal of Magnetic Resonance. Mar2010, Vol. 203 Issue 1, p52-56. 5p.
Subjects:	Molecule-molecule collisions, Nuclear magnetic resonance spectroscopy, Polarization (Nuclear physics), Transients (Dynamics), Ligand binding (Biochemistry), Enzyme inhibitors
Abstract:	Abstract: NMR spectroscopy is an established, versatile technique for the detection of molecular interactions, even when these interactions are weak. Signal enhancement by several orders of magnitude through dynamic nuclear polarization alleviates several practical limitations of NMR-based interaction studies. This enhanced non-equilibrium polarization contributes sensitivity for the detection of molecular interactions in a single NMR transient. We show that direct 13C NMR ligand binding studies at natural isotopic abundance of 13C gets feasible in this way. Resultant screens are easy to interpret and can be performed at 13C concentrations below μM. In addition to such ligand-detected studies of molecular interaction, ligand binding can be assessed and quantified with enzymatic assays that employ hyperpolarized substrates at varying enzyme inhibitor concentrations. The physical labeling of nuclear spins by hyperpolarization thus provides the opportunity to devise fast novel in vitro experiments with low material requirement and without the need for synthetic modifications of target or ligands. [Copyright &y& Elsevier]
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Database:	Engineering Source

Description
Abstract:	Abstract: NMR spectroscopy is an established, versatile technique for the detection of molecular interactions, even when these interactions are weak. Signal enhancement by several orders of magnitude through dynamic nuclear polarization alleviates several practical limitations of NMR-based interaction studies. This enhanced non-equilibrium polarization contributes sensitivity for the detection of molecular interactions in a single NMR transient. We show that direct 13C NMR ligand binding studies at natural isotopic abundance of 13C gets feasible in this way. Resultant screens are easy to interpret and can be performed at 13C concentrations below μM. In addition to such ligand-detected studies of molecular interaction, ligand binding can be assessed and quantified with enzymatic assays that employ hyperpolarized substrates at varying enzyme inhibitor concentrations. The physical labeling of nuclear spins by hyperpolarization thus provides the opportunity to devise fast novel in vitro experiments with low material requirement and without the need for synthetic modifications of target or ligands. [Copyright &y& Elsevier]
ISSN:	10907807
DOI:	10.1016/j.jmr.2009.11.020