| Literature DB >> 19780183 |
Yann Jamin1, Cristina Gabellieri, Lynette Smyth, Steven Reynolds, Simon P Robinson, Caroline J Springer, Martin O Leach, Geoffrey S Payne, Thomas R Eykyn.
Abstract
Carboxypeptidase G2 (CPG2) is a bacterial enzyme that is currently employed in a range of targeted cancer chemotherapy strategies such as gene-directed enzyme prodrug therapy (GDEPT). Employing dynamic nuclear polarization (DNP) and natural abundance (13)C magnetic resonance spectroscopy (MRS), we observed the CPG2-mediated conversion of a novel hyperpolarized reporter probe 3,5-difluorobenzoyl-L-glutamic acid (3,5-DFBGlu) to 3,5-difluorobenzoic acid (3,5-DFBA) and L-glutamic acid (L-Glu) in vitro. Isotopic labeling of the relevant nuclei with (13)C in 3,5-DFBGlu or related substrates will yield a further factor of 100 increase in the signal-to-noise. We discuss the feasibility of translating these experiments to generate metabolic images of CPG2 activity in vivo. (c) 2009 Wiley-Liss, Inc.Entities:
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Year: 2009 PMID： 19780183 DOI： 10.1002/mrm.22049
Source DB: PubMed Journal: Magn Reson Med ISSN： 0740-3194 Impact factor: 4.668