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| Home > Publications database > Binding of TCA to the prion protein: mechanism, implication for therapy, and application as probe for complex formation of bio-macromolecules > print |
| 001 | 6512 | ||
| 005 | 20200402205709.0 | ||
| 024 | 7 | _ | |2 WOS |a WOS:000270000500006 |
| 037 | _ | _ | |a PreJuSER-6512 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Mangels, C. |b 0 |
| 245 | _ | _ | |a Binding of TCA to the prion protein: mechanism, implication for therapy, and application as probe for complex formation of bio-macromolecules |
| 260 | _ | _ | |a Guilderland, NY |b Adenine Press |c 2009 |
| 300 | _ | _ | |a 163 - 170 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |0 16381 |a Journal of Biomolecular Structure & Dynamics |v 27 |x 0739-1102 |y 2 |
| 500 | _ | _ | |a We 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. |
| 520 | _ | _ | |a Tricyclic 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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| 650 | _ | 7 | |2 WoSType |a J |
| 653 | 2 | 0 | |2 Author |a Conformational disease |
| 653 | 2 | 0 | |2 Author |a Prion protein |
| 653 | 2 | 0 | |2 Author |a Quinacrine |
| 653 | 2 | 0 | |2 Author |a 9-aminoacridine |
| 653 | 2 | 0 | |2 Author |a Drug design |
| 653 | 2 | 0 | |2 Author |a Ligand binding |
| 653 | 2 | 0 | |2 Author |a NMR-spectroscopy |
| 653 | 2 | 0 | |2 Author |a in vitro binding assay |
| 653 | 2 | 0 | |2 Author |a Relaxation |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Frank, A.O. |b 1 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Ziegler, J. |b 2 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Klingenstein, R. |b 3 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Schweimer, K. |b 4 |
| 700 | 1 | _ | |0 P:(DE-Juel1)132029 |a Willbold, D. |b 5 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Korth, C. |b 6 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Rösch, P. |b 7 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Schwarzinger, S. |b 8 |
| 773 | _ | _ | |0 PERI:(DE-600)2085732-9 |g Vol. 27, p. 163 - 170 |p 163 - 170 |q 27<163 - 170 |t Journal of biomolecular structure & dynamics |v 27 |x 0739-1102 |y 2009 |
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| 914 | 1 | _ | |y 2009 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |d 31.12.2010 |g ISB |k ISB-3 |l Strukturbiochemie |0 I:(DE-Juel1)VDB942 |x 0 |
| 920 | 1 | _ | |0 I:(DE-82)080012_20140620 |k JARA-HPC |l Jülich Aachen Research Alliance - High-Performance Computing |g JARA |x 1 |
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| 980 | _ | _ | |a UNRESTRICTED |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
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| 981 | _ | _ | |a I:(DE-Juel1)VDB1346 |
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