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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

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

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

  • 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