NR AOTT
AU Hänel,K.; Smolinski,J.; König,B.W.; Willbold,D.
TI Stabilization of PrPc conformation as a potential way to TSE therapy
QU International Conference - Prion diseases: from basic research to intervention concepts - TSE-Forum, 08.10.-10.10.2003, Gasteig, München - Poster session - IV-03
PT Konferenz-Poster
AB The prion-model of transmissible spongioform encephalopathies (TSE) is based on the essential role of the host-encoded prion-protein (PrP). Whatever the details of the special formulation of the prion model may be ("protein-only"-hypothesis, heterodimer-model, seeded polymerization), a conformational change of PrPc into PrPsc is always assumed as a crucial step for the propagation of infection units. Development and progression of the disease implies ongoing conversion of PrPc into PrPsc. Any stabilization of the PrPc conformation may be expected to slow down or inhibit conversion of PrPc into PrPsc. Based on these considerations, we will present the first results from a project that was planned to identify substances, that tightly bind PrPc with high specificity. We expect these substances to stabilize the PrPc conformation in order to impair the conversion of PrPc into PrPsc or even reverse it.
AD Karen Hänel, Bernd W. König, Dieter Willbold, Forschungszentrum, Jülich, Germany; Karen Hänel, Bernd W. König, Dieter Willbold, Heinrich-Heine-Universität, Düsseledorf, Germany; Jörg Smolinski, Dieter Willbold, Institut für Molekulare Biotechnologie, Jena, Germany
SP englisch
PO Deutschland