Inhibition of Acetylcholinesterase and Butyrylcholinesterase by a Plant Secondary Metabolite Boldine
Jazyk angličtina Země Spojené státy americké Médium electronic-ecollection
Typ dokumentu časopisecké články
PubMed
29850593
PubMed Central
PMC5907398
DOI
10.1155/2018/9634349
Knihovny.cz E-zdroje
- MeSH
- acetylcholinesterasa metabolismus MeSH
- aporfiny chemie farmakologie MeSH
- butyrylcholinesterasa chemie metabolismus MeSH
- cholinesterasové inhibitory chemie farmakologie MeSH
- HEK293 buňky MeSH
- lidé MeSH
- molekulární modely MeSH
- sekundární metabolismus * MeSH
- substrátová specifita účinky léků MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- acetylcholinesterasa MeSH
- aporfiny MeSH
- boldine MeSH Prohlížeč
- butyrylcholinesterasa MeSH
- cholinesterasové inhibitory MeSH
Acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) are two enzymes sensitive to various chemical compounds having ability to bind to crucial parts of these enzymes. Boldine is a natural alkaloid and it was mentioned in some older works that it can inhibit some kinds of AChE. We reinvestigated this effect on AChE and also on BChE using acetyl (butyryl) thiocholine and Ellman's reagents as standard substances for spectrophotometric assay. We found out IC50 of AChE equal to 372 μmol/l and a similar level to BChE, 321 μmol/l. We conclude our experiment by a finding that boldine is cholinesterase inhibitor; however we report significantly weaker inhibition than that suggested in literature. Likewise, we tried to investigate the mechanism of inhibition and completed it with in silico study. Potential toxic effect on cholinesterases in real conditions is also discussed.
Faculty of Chemical Technology University of Pardubice 532 10 Pardubice Czech Republic
Faculty of Military Health Sciences University of Defence 500 10 Hradec Kralove Czech Republic
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