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Hyperpolarized 13C magnetic resonance detection of carboxypeptidase G2 activity

✍ Scribed by Yann Jamin; Cristina Gabellieri; Lynette Smyth; Steven Reynolds; Simon P. Robinson; Caroline J. Springer; Martin O. Leach; Geoffrey S. Payne; Thomas R. Eykyn

Publisher
John Wiley and Sons
Year
2009
Tongue
English
Weight
348 KB
Volume
62
Category
Article
ISSN
0740-3194

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✦ Synopsis

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. Magn Reson Med, 2009. © 2009 Wiley‐Liss, Inc.

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