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Abstract #3371

Chemical Exchange Saturation Transfer on a prototype model of neurodegeneration.

Eleni Demetriou 1 , Andreia C Silva 1 , Marilena Rega 1 , Francisco Torrealdea 1 , James E M Fairney 1,2 , Mohamed Tachrount 1 , Mark Farrow 3 , and Xavier Golay 1

1 Brain repair and rehabilitation, Institute of Neurology, London, United Kingdom, 2 Medical Physics &Biomedical engineering, University College of London, London, United Kingdom, 3 MRC prion unit, UCL Institute of Neurology, London, United Kingdom

In this study, we apply Chemical Exchange Saturation Transfer (CEST) to examine changes related to protein folding and aggregation occurring in a terminal mouse model of prion disease. A trend towards increased amide proton transfer in the Prion mice was found in the cortex and basal ganglia but was not statistically significant .However, this was also accompanied by a significant reduction found in the magnetization transfer asymmetry at 10μT power in both basal ganglia and cortex of the diseased animals, suggestive of changes happening in the local proteasome possibly indicating cell death at this late stage of this disease, in addition to a reduced number of exposed amine groups due to PrP misfolding.

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