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Abstract #3163

MR imaging of protein folding employing NuclearOverhausermediated saturation transfer

Patrick Kunz 1 , Moritz Zaiss 2 , Steffen Goerke 2 , Alexander Radbruch 3,4 , and Peter Bachert 2

1 Division of Functional Genome Analysis, German Cancer Research Center (DKFZ), Heidelberg, Germany, 2 Dept. Medical Physics in Radiology, German Cancer Research Center (DKFZ), Heidelberg, Germany, 3 Dept. of Neuroradiology, University of Heidelberg, Heidelberg, Germany, 4 Section Neurooncologic Imaging, German Cencer Research Center (DKFZ), Heidelberg, Germany

Ureadependent unfolding of BSA, which can be monitored by fluorescence spectroscopy, affects saturation transfer between water and aliphatic protons of the protein mediated by dipoledipole couplings (NOE). We show that the NOE imaging contrast of the BSA solution is a function of protein structure and propose that, besides concentration, temperature, and pH, protein folding/unfolding generates an additional contrast mechanism of CEST MR imaging. First outcomes of application in human glioblastoma patients are presented and discussed.

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