NR AUSV
AU Fransson,L.; Elfrink,K.; Riesner,D.; Willbold,D.
TI Therapy of Transmissible Spongiform Encephalopathies with PrP-binding Peptides selected by Phage Display
QU TSE-Forum, 6. Kongress - Nationale TSE-Forschungsplattform, Greifswald 26.6.-28.6.2006, Poster: Therapie THE-01
PT Konferenz-Poster
AB
Transmissible spongiform encephalopathies are fatal neurodegenerative diseases that can affect humans as well as animals. The disease-causing agent is the pathogenic isoform of the prion protein (PrP). PrP is a cellular protein located on the exterior cell surface. It is attached to the plasma membrane via a glycosylphosphatidylinositol (GPI) anchor. The pathogenic isoform of PrP is mainly ß-structured in contrast to the predominantly alpha-helical cellular isoform of PrP. Since ß-structured PrP is needed for infectivity, the conversion of alpha-helical conformation into ß-structured PrP is thought to be the key event in the pathogenesis of TSE. An inhibition of this conversion by stabilization of the cellular isoform might be an approach to prevention or even therapy of TSE.
We focus on such stabilization by PrP ligands that bind specifically to the cellular isoform. Here, we present the selection of PrP-binding peptides. The selection was performed by using phage display with membrane anchored cellular PrP from CHO-cells as target. The identified peptides have to be synthesized. Their ability to bind cellular PrP will be examined by NMR spectroscopy and surface plasmon resonance (SPR). In vitro and in vivo tests will be performed to investigate the capacity of the selected peptides to stabilize the cellular isoform of PrP.
AD Lisa Fransson, Kerstin Elfrink, Detlev Riesner, Dieter Willbold, Institut für Physikalische Biologie, Heinrich-Heine-Universität Düsseldorf, Germany D-40225; Lisa Fransson, Dieter Willbold, Forschungszentrum Jülich IBI-2, Jülich, Germany D-52425
SP englisch
PO Deutschland
OR Tagungsband