Tetrafluorination of sugars as strategy for enhancing protein-carbohydrate affinity: application to UDP-Galp mutase inhibition.

Authors :: N'Go I
Golten S
Ardá A
Cañada J
Jiménez-Barbero J
Linclau B
Vincent SP
Source :: Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2014 Jan 03; Vol. 20 (1), pp. 106-12. Date of Electronic Publication: 2013 Dec 05.
Publication Year :: 2014
Abstract: Tetrafluorinated analogues of both UDP-galactopyranose and UDP-galactofuranose have been synthesized and assayed against UDP-galactopyranose mutase, a key enzyme for Mycobacterium tuberculosis cell wall biosynthesis. Competition assays and STD-NMR spectroscopy techniques have evidenced not only the first unambiguous case of affinity enhancement through local sugar polyfluorination, but also showed that tetrafluorination can still have a beneficial effect on binding when monofluorination at the same position does not.<br /> (Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Subjects :: Bacterial Proteins antagonists & inhibitors
Biocatalysis
Carbohydrates chemistry
Enzyme Inhibitors chemistry
Enzyme Inhibitors metabolism
Fluorine chemistry
Galactose analogs & derivatives
Galactose chemistry
Galactose metabolism
Halogenation
Intramolecular Transferases antagonists & inhibitors
Magnetic Resonance Spectroscopy
Mycobacterium tuberculosis enzymology
Protein Binding
Uridine Diphosphate analogs & derivatives
Uridine Diphosphate chemistry
Uridine Diphosphate metabolism
Bacterial Proteins metabolism
Intramolecular Transferases metabolism

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