Quinacrine reactivity with prion proteins and prion-derived peptides
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F13%3A10189619" target="_blank" >RIV/00216208:11110/13:10189619 - isvavai.cz</a>
Alternative codes found
RIV/61388963:_____/13:00392499
Result on the web
<a href="http://dx.doi.org/10.1007/s00726-013-1460-x" target="_blank" >http://dx.doi.org/10.1007/s00726-013-1460-x</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s00726-013-1460-x" target="_blank" >10.1007/s00726-013-1460-x</a>
Alternative languages
Result language
angličtina
Original language name
Quinacrine reactivity with prion proteins and prion-derived peptides
Original language description
Quinacrine is a drug that is known to heal neuronal cell culture infected with prions, which are the causative agents of neurodegenerative diseases called transmissible spongiform encephalopathies. However, the drug fails when it is applied in vivo. In this work, we analyzed the reason for this failure. The drug was suggested to "covalently" modify the prion protein via an acridinyl exchange reaction. To investigate this hypothesis more closely, the acridine moiety of quinacrine was covalently attachedto the thiol groups of cysteines belonging to prion-derived peptides and to the full-length prion protein. The labeled compounds were conveniently monitored by fluorescence and absorption spectroscopy in the ultraviolet and visible spectral regions. Theacridine moiety demonstrated characteristic UV-vis spectrum, depending on the substituent at the C-9 position of the acridine ring. These results confirm that quinacrine almost exclusively reacts with the thiol groups present in proteins
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EE - Microbiology, virology
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GA203%2F07%2F1517" target="_blank" >GA203/07/1517: Chemical syntheses of fluorescence labeled mouse prion proteins using chemical ligations and investigation of their properties</a><br>
Continuities
S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Amino Acids
ISSN
0939-4451
e-ISSN
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Volume of the periodical
44
Issue of the periodical within the volume
5
Country of publishing house
AT - AUSTRIA
Number of pages
14
Pages from-to
1279-1292
UT code for WoS article
000317682100004
EID of the result in the Scopus database
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