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

Content Provider	Springer Nature Link
Author	Zawada, Zbigniew Šafařík, Martin Dvořáková, Eva Jaušková, Olga Březivá, Anna Stibor, Ivan Holada, Karel Bouř, Petr Hlaváček, Jan Šebestík, Jaroslav
Copyright Year	2013
Abstract	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 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.
Starting Page	1279
Ending Page	1292
Page Count	14
File Format	PDF
ISSN	09394451
Journal	Amino Acids
Volume Number	44
Issue Number	5
e-ISSN	14382199
Language	English
Publisher	Springer Vienna
Publisher Date	2013-01-23
Publisher Place	Vienna
Access Restriction	Subscribed
Subject Keyword	Quinacrine Prion protein and peptide model reactions Solid phase and recombinant synthesis Biochemistry Analytical Chemistry Biochemical Engineering Life Sciences Proteomics Neurobiology
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry Clinical Biochemistry

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