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Isoquinoline alkaloids as prolyl oligopeptidase inhibitors
L. Cahlíková, L. Hulová, M. Hrabinová, J. Chlebek, A. Hošťálková, M. Adamcová, M. Šafratová, D. Jun, L. Opletal, M. Ločárek, K. Macáková,
Fitoterapia.
2015 ;
103 (-) :
192-6.
[pub] 20150409
Language English Country Netherlands
Document type Journal Article, Research Support, Non-U.S. Gov't
Persistent link
https://www.medvik.cz/link/bmc15031397
- MeSH
- Alkaloids chemistry MeSH
- Aporphines chemistry MeSH
- Dioxoles chemistry MeSH
- Heterocyclic Compounds, 4 or More Rings chemistry MeSH
- Serine Proteinase Inhibitors chemistry MeSH
- Isoquinolines chemistry MeSH
- Molecular Structure MeSH
- Serine Endopeptidases chemistry MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
Prolyl oligopeptidase is a cytosolic serine peptidase that hydrolyses proline-containing peptides at the carboxy terminus of proline residues. It has been associated with schizophrenia, bipolar affective disorder, and related neuropsychiatric disorders and therefore may have important clinical implications. Thirty-one isoquinoline alkaloids of various structural types, previously isolated in our laboratory, were screened for their ability to inhibit prolyl oligopeptidase. Promising results have been showed by alkaloids californidine (IC50=55.6±3.5 μM), dihydrosanquinarine (IC50=99.1±7.6 μM), corypalmine (IC50=128.0±10.5 μM) and N-methyllaurotetanine (IC50=135.0±11.7 μM).
References provided by Crossref.org
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