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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 lower case Greek beta -cyclodextrin.

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