Quinacrine reactivity with prion proteins and prion-derived peptides

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/61388963:_____/13:00392499

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Quinacrine reactivity with prion proteins and prion-derived peptides

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

Quinacrine reactivity with prion proteins and prion-derived peptides

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

<a href="/cs/project/GA203%2F07%2F1517" target="_blank" >GA203/07/1517: Chemická syntéza fluorescenčně značených myších prionových proteinů využívající chemické ligace a studium jejich vlastností</a><br>

Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Amino Acids

ISSN

0939-4451

e-ISSN

—

Svazek periodika

44

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

AT - Rakouská republika

Počet stran výsledku

14

Strana od-do

1279-1292

Kód UT WoS článku

000317682100004

EID výsledku v databázi Scopus

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