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Statements

Subject Item
n2:RIV%2F00216208%3A11110%2F13%3A10189619%21RIV14-GA0-11110___
rdf:type
n6:Vysledek skos:Concept
rdfs:seeAlso
http://dx.doi.org/10.1007/s00726-013-1460-x
dcterms: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 %22covalently%22 modify the prion protein via an acridinyl exchange reaction. To investigate this hypothesis more closely, the acridine moiety of quinacrine was covalently attached to 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. The acridine 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 and peptides. The chemical reaction alters the prion properties and increases the concentration of the acridine moiety in the prion protein. 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 %22covalently%22 modify the prion protein via an acridinyl exchange reaction. To investigate this hypothesis more closely, the acridine moiety of quinacrine was covalently attached to 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. The acridine 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 and peptides. The chemical reaction alters the prion properties and increases the concentration of the acridine moiety in the prion protein.
dcterms:title
Quinacrine reactivity with prion proteins and prion-derived peptides Quinacrine reactivity with prion proteins and prion-derived peptides
skos:prefLabel
Quinacrine reactivity with prion proteins and prion-derived peptides Quinacrine reactivity with prion proteins and prion-derived peptides
skos:notation
RIV/00216208:11110/13:10189619!RIV14-GA0-11110___
n6:predkladatel
n20:orjk%3A11110
n3:aktivita
n15:S n15:P n15:I
n3:aktivity
I, P(GA203/07/1517), S
n3:cisloPeriodika
5
n3:dodaniDat
n19:2014
n3:domaciTvurceVysledku
n10:3042367 n10:6307337 n10:8564078
n3:druhVysledku
n11:J
n3:duvernostUdaju
n21:S
n3:entitaPredkladatele
n7:predkladatel
n3:idSjednocenehoVysledku
101279
n3:idVysledku
RIV/00216208:11110/13:10189619
n3:jazykVysledku
n12:eng
n3:klicovaSlova
Solid phase and recombinant synthesis; Prion protein and peptide model reactions; Quinacrine
n3:klicoveSlovo
n9:Prion%20protein%20and%20peptide%20model%20reactions n9:Quinacrine n9:Solid%20phase%20and%20recombinant%20synthesis
n3:kodStatuVydavatele
AT - Rakouská republika
n3:kontrolniKodProRIV
[E885F11513E4]
n3:nazevZdroje
Amino Acids
n3:obor
n17:EE
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
10
n3:projekt
n13:GA203%2F07%2F1517
n3:rokUplatneniVysledku
n19:2013
n3:svazekPeriodika
44
n3:tvurceVysledku
Janoušková, Olga Sebestik, Jaroslav Brezinova, Anna Šafařík, Martin Zawada, Zbigniew Dvořáková, Eva Hlavacek, Jan Stibor, Ivan Bour, Petr Holada, Karel
n3:wos
000317682100004
s:issn
0939-4451
s:numberOfPages
14
n4:doi
10.1007/s00726-013-1460-x
n18:organizacniJednotka
11110