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000006512 084__ $$2WoS$$aBiochemistry & Molecular Biology
000006512 084__ $$2WoS$$aBiophysics
000006512 1001_ $$0P:(DE-HGF)0$$aMangels, C.$$b0
000006512 245__ $$aBinding of TCA to the prion protein: mechanism, implication for therapy, and application as probe for complex formation of bio-macromolecules
000006512 260__ $$aGuilderland, NY$$bAdenine Press$$c2009
000006512 300__ $$a163 - 170
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000006512 440_0 $$016381$$aJournal of Biomolecular Structure & Dynamics$$v27$$x0739-1102$$y2
000006512 500__ $$aWe thank Dr. Vilma Martins for providing a plasmid with the human PRNP-gene. Financial support from the Bavarian Prion Research Platform (ForPrion) and the Volkswagen-Stiftung (1/79968) is gratefully acknowledged.
000006512 520__ $$aTricyclic aromatic compounds (TCA) are promising candidates for treatment of transmissible spongiform encephalopathies. Direct binding to the cellular prion protein (PrPC) has been proposed as anti-prion active mechanism. We here show by means of NMR-spectroscopy that binding of TCA occurs with millimolar affinity to motifs consisting of two neighboring aromatic residues (Ar-Ar motif). It is independent of the secondary structure of this motif and of the side chain attached to the TCA and it is not specific to PrPC. Because biologically inactive 9-aminoacridine (9-aa) binds with similar K-D as anti-prion active quinacrine, direct interaction with PrPC as mechanism of action appears highly unlikely. However, binding of 9-aa to Ar-Ar-motifs in proteins can be used as reporter for biological macromolecule interactions, by measuring changes in T-1-NMR relaxation times of 9-aa.
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000006512 65320 $$2Author$$aConformational disease
000006512 65320 $$2Author$$aPrion protein
000006512 65320 $$2Author$$aQuinacrine
000006512 65320 $$2Author$$a9-aminoacridine
000006512 65320 $$2Author$$aDrug design
000006512 65320 $$2Author$$aLigand binding
000006512 65320 $$2Author$$aNMR-spectroscopy
000006512 65320 $$2Author$$ain vitro binding assay
000006512 65320 $$2Author$$aRelaxation
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000006512 7001_ $$0P:(DE-HGF)0$$aFrank, A.O.$$b1
000006512 7001_ $$0P:(DE-HGF)0$$aZiegler, J.$$b2
000006512 7001_ $$0P:(DE-HGF)0$$aKlingenstein, R.$$b3
000006512 7001_ $$0P:(DE-HGF)0$$aSchweimer, K.$$b4
000006512 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b5$$uFZJ
000006512 7001_ $$0P:(DE-HGF)0$$aKorth, C.$$b6
000006512 7001_ $$0P:(DE-HGF)0$$aRösch, P.$$b7
000006512 7001_ $$0P:(DE-HGF)0$$aSchwarzinger, S.$$b8
000006512 773__ $$0PERI:(DE-600)2085732-9$$gVol. 27, p. 163 - 170$$p163 - 170$$q27<163 - 170$$tJournal of biomolecular structure & dynamics$$v27$$x0739-1102$$y2009
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