Abstract #2780
Hyperpolarization of a bisfluorinated phenylalanine derivative using PHIP and examination of the interaction with -cyclodextrin
Markus Plaumann 1 , Thomas Trantzschel 1 , Denise Lego 2 , Claudia Khn 1 , Grit Sauer 3 , Torsten Gutmann 3 , Joachim Bargon 4 , Gerd Buntkowsky 3 , Ute Bommerich 2 , and Johannes Bernarding 1
1
Department for Biometrics und Medical
Informatics, Otto-von-Guericke-University Magdeburg,
Magdeburg, Saxony-Anhalt, Germany,
2
Special
Lab Non-Invasive Brain Imaging, Leibniz Institute for
Neurobiology, Magdeburg, Saxony-Anhalt, Germany,
3
Institute
for Physical Chemistry, Technical University Darmstadt,
Darmstadt, Hesse, Germany,
4
Institute of
Physical and Theoretical Chemistry, University Bonn,
Bonn, North Rhine-Westphalia, Germany
Amino acids are highly relevant in biological pathways
and for protein and enzyme structures or for the
synthesis of neurotransmitter. An essential amino acid
is L-phenylalanine (Phe). The use of fluorinated amino
acids are of great interest in medical chemistry and
diagnostics especially for the investigation of amino
acid metabolism, protein structures and protein-ligand
interactions. The disadvantage of low spin density in
vivo can be overcome by hyperpolarization methods like
Parahydrogen Induced Polarization. We present the
hyperpolarization of a bisfluorinated phenylalanine
derivative and studies of the interaction between Phe
and
-cyclodextrin.
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