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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