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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F14%3A00433505" target="_blank" >RIV/61388971:_____/14:00433505 - isvavai.cz</a>

Alternative codes found

RIV/67179843:_____/14:00433505 RIV/61388963:_____/14:00433505

Result on the web

<a href="http://dx.doi.org/10.3390/molecules19033471" target="_blank" >http://dx.doi.org/10.3390/molecules19033471</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/molecules19033471" target="_blank" >10.3390/molecules19033471</a>

Result language

angličtina

Original language name

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

Original language description

NAG-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

Czech name

—

Czech description

—

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

—

Project

—

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2014

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Molecules

ISSN

1420-3049

e-ISSN

—

Volume of the periodical

19

Issue of the periodical within the volume

3

Country of publishing house

CH - SWITZERLAND

Number of pages

18

Pages from-to

3471-3488

UT code for WoS article

000335826800049

EID of the result in the Scopus database

—