Synthesis of modified D-mannose core derivatives and their impact on GH38 α-mannosidases
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články
PubMed
27152630
DOI
10.1016/j.carres.2016.04.004
PII: S0008-6215(16)30100-8
Knihovny.cz E-zdroje
- Klíčová slova
- GH38 family, Golgi α-mannosidase, Inhibition, Lysosomal α-mannosidase, α-Mannosidase inhibitor,
- MeSH
- Drosophila melanogaster enzymologie genetika MeSH
- inhibitory enzymů chemická syntéza chemie farmakologie MeSH
- lidé MeSH
- lyzozomy enzymologie MeSH
- mannosa chemie MeSH
- mannosidasy antagonisté a inhibitory genetika MeSH
- molekulární modely MeSH
- proteiny Drosophily antagonisté a inhibitory genetika MeSH
- rekombinantní proteiny metabolismus MeSH
- vazebná místa MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- inhibitory enzymů MeSH
- mannosa MeSH
- mannosidasy MeSH
- proteiny Drosophily MeSH
- rekombinantní proteiny MeSH
Nine new compounds having five- and modified six-member carbohydrate core derived from D-lyxose or D-mannose, and non-hydrolysable aglycones (benzylsulfonyl or aryl(alkyl)triazolyl) were synthesised to investigate their ability to inhibit the recombinant Drosophila melanogaster homologs of two human GH38 family enzymes: Golgi mannosidase II (dGMIIb) and lysosomal mannosidase (dLMII). Two compounds were weak selective dGMIIb inhibitors showing IC50 at mM level. Moreover, it was found that another GH38 enzyme, commercial jack bean α-mannosidase, was inhibited by triazole conjugates regardless of the carbohydrate core while the corresponding sulfones were inactive.
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