Počet záznamů: 1  

Inhibition of GlcNAc-Processing Glycosidases by C-6-Azido-NAG-Thiazoline and Its Derivatives

  1. 1.
    SYSNO ASEP0433505
    Druh ASEPJ - Článek v odborném periodiku
    Zařazení RIVJ - Článek v odborném periodiku
    Poddruh JČlánek ve WOS
    NázevInhibition of GlcNAc-Processing Glycosidases by C-6-Azido-NAG-Thiazoline and Its Derivatives
    Tvůrce(i) Krejzová, Jana (MBU-M) RID
    Šimon, Petr (MBU-M)
    Ježová-Kalachová, Lubica (MBU-M) RID
    Kulik, Natallia (UEK-B) RID
    Bojarová, Pavla (MBU-M) ORCID
    Marhol, Petr (MBU-M) RID
    Pelantová, Helena (MBU-M) ORCID, RID
    Cvačka, Josef (UOCHB-X) RID, ORCID
    Ettrich, Rüdiger (UEK-B) RID, ORCID, SAI
    Slámová, Kristýna (MBU-M) RID, ORCID
    Křen, Vladimír (MBU-M) RID, ORCID
    Zdroj.dok.Molecules. - : MDPI - ISSN 1420-3049
    Roč. 19, č. 3 (2014), s. 3471-3488
    Poč.str.18 s.
    Jazyk dok.eng - angličtina
    Země vyd.CH - Švýcarsko
    Klíč. slovaNAG-thiazoline ; enzyme inhibition ; O-GlcNAcase
    Vědní obor RIVCE - Biochemie
    Institucionální podporaMBU-M - RVO:61388971 ; RVO:67179843 - RVO:67179843 ; UOCHB-X - RVO:61388963
    UT WOS000335826800049
    DOI https://doi.org/10.3390/molecules19033471
    AnotaceNAG-thiazoline is a strong competitive inhibitor of GH20 beta-N-acetylhexosaminidases and GH84 beta-N-acetylglucosaminidases. Here, we focused on the design, synthesis and inhibition potency of a series of new derivatives of NAG-thiazoline modified at the C-6 position. Dimerization of NAG-thiazoline via C-6 attached triazole linkers prepared by click chemistry was employed to make use of multivalency in the inhibition. Novel compounds were tested as potential inhibitors of beta-N-acetylhexosaminidases from Talaromyces flavus, Streptomyces plicatus (both GH20) and beta-N-acetylglucosaminidases from Bacteroides thetaiotaomicron and humans (both GH84). From the set of newly prepared NAG-thiazoline derivatives, only C-6-azido-NAG-thiazoline displayed inhibition activity towards these enzymes; C-6 triazole-substituted NAG-thiazolines lacked inhibition activity against the enzymes used. Docking of C-6-azido-NAG-thiazoline into the active site of the tested enzymes was performed. Moreover, a stability study with GlcNActhiazoline confirmed its decomposition at pH < 6 yielding 2-acetamido-2-deoxy-1-thio-alpha/beta-D-glucopyranoses, which presumably dimerize oxidatively into S-S linked dimers; decomposition products of NAG-thiazoline are void of inhibitory activity
    PracovištěMikrobiologický ústav
    KontaktEliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
    Rok sběru2015
Počet záznamů: 1  

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