About: Quinacrine reactivity with prion proteins and prion-derived peptides

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An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://dx.doi.org/10.1007/s00726-013-1460-x
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. (en)
Title	Quinacrine reactivity with prion proteins and prion-derived peptides Quinacrine reactivity with prion proteins and prion-derived peptides (en)
skos:prefLabel	Quinacrine reactivity with prion proteins and prion-derived peptides Quinacrine reactivity with prion proteins and prion-derived peptides (en)
skos:notation	RIV/00216208:11110/13:10189619!RIV14-GA0-11110___
http://linked.open...avai/riv/aktivita	I P S
http://linked.open...avai/riv/aktivity	I, P(GA203/07/1517), S
http://linked.open...iv/cisloPeriodika	5
http://linked.open...vai/riv/dodaniDat	2014
http://linked.open...aciTvurceVysledku	Dvořáková, Eva Janoušková, Olga Holada, Karel
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Karlova v Praze / 1. lékařská fakulta
http://linked.open...dnocenehoVysledku	101279
http://linked.open...ai/riv/idVysledku	RIV/00216208:11110/13:10189619
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Solid phase and recombinant synthesis; Prion protein and peptide model reactions; Quinacrine (en)
http://linked.open.../riv/klicoveSlovo	Prion protein and peptide model reactions Quinacrine Solid phase and recombinant synthesis
http://linked.open...odStatuVydavatele	AT - Rakouská republika
http://linked.open...ontrolniKodProRIV	[E885F11513E4]
http://linked.open...i/riv/nazevZdroje	Amino Acids
http://linked.open...in/vavai/riv/obor	EE
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	10 (xsd:int)
http://linked.open...vavai/riv/projekt	Chemical syntheses of fluorescence labeled mouse prion proteins using chemical ligations and investigation of their properties
http://linked.open...UplatneniVysledku	2013
http://linked.open...v/svazekPeriodika	44
http://linked.open...iv/tvurceVysledku	Holada, Karel Dvořáková, Eva Janoušková, Olga Zawada, Zbigniew Šafařík, Martin Stibor, Ivan Bour, Petr Brezinova, Anna Hlavacek, Jan Sebestik, Jaroslav
http://linked.open...ain/vavai/riv/wos	000317682100004
issn	0939-4451
number of pages	14 (xsd:int)
http://bibframe.org/vocab/doi	10.1007/s00726-013-1460-x
http://localhost/t...ganizacniJednotka	11110

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