NR AOSQ
AU Frank,A.; Ziegler,J.; Leliveld,S.R.; Korth,C.; Rösch,P.; Schwarzinger,S.
TI Evidence for Binding of Tricyclic Aromatic Compounds to Helix 1 of PrP
QU International Conference - Prion diseases: from basic research to intervention concepts - TSE-Forum, 08.10.-10.10.2003, Gasteig, München - Poster session - IV-24
PT Konferenz-Poster
AB
Tricyclic aromatic compounds - such as quinacrine - have been suggested as therapeutic drugs in treatment of prion diseases (1). However, neither the mechanisms of how these compounds act nor the molecular targets for these substances are known. Here we present an NMR- and CD-spectroscopic study providing evidence that tricyclic aromatic compounds can bind to PrP-helix 1 peptides, which are rich in aromatic amino acid residues that are even partially exposed in the solution structure of prion protein. CD-spectroscopy also indicates interaction with full length PrP. We discuss a model for binding of tricyclic aromatic compounds to PrP and its implications on rational drug design.
(1) Korth et al.(2001) Proc. Natl. Acad. Sci. U. S. A. 98, 9836-9841.
AD Andreas Frank, Jan Ziegler, Paul Rösch, Stephan Schwarzinger, University Bayreuth - Lehrstuhl Biopolymere, Germany; Rutger Leliveld, Carsten Korth, Heinrich Heine University Düsseldorf - Institute for Neuropathology, Germany
SP englisch
PO Deutschland