NR ATNW
AU Fransson,L.; Hänel,K.; Willbold,D.
TI Therapy of Transmissible Spongiform Encephalopathies with PrP-binding Peptides selected by Phage Display
QU International Conference - Prion 2005: Between fundamentals and society's needs - 19.10.-21.10.2005, Congress Center Düsseldorf - Poster Session: Human prions, risk of blood products, and therapy HUMAN-20
PT Konferenz-Poster
AB
In contrast to the cellular predominantly alpha-helical isoform of prion protein, the disease associated PrP is mainly ß-structured. The conversion of PrP from the alpha-helical conformation into the ß-structured isoform plays a decisive role in the course of TSEs. Fibrillary ß-structured PrP seems to be essential for infectivity and is presumably the exclusive cause of the disease. Therefore, stabilization of the cellular isoform and inhibition of the conversion into the ß-structured state may be a suitable approach for prevention or therapy of prion diseases. We focus on such stabilization by PrP ligands that bind specifically to the cellular isoform.
We will present PrP-binding peptides, which were identified by using phage display with membrane anchored cellular PrP as target. The identified peptides are to be synthesized and their ability to inhibit the conversion of PrP into the ß-structured isoform will be examined by NMR spectroscopy and surface plasmon resonance.
AD L.Fransson, K.Hänel, D.Willbold, Institut für Physikalische Biologie, Heinrich-Heine-Universität Düsseldorf, Germany D-40225 und Forschungszentrum Jülich IBI-2, Jülich, Germany D-52425
SP englisch
PO Deutschland