The ability to custom-modify cell surface glycans holds great promise for treatment of a variety of diseases. We propose a glycomimetic ofl-fucose that markedly inhibits the creation of sLeXby FTVI and FTVII, but has no effect on creation of LeXby FTIX. Our findings thus indicate that selective suppression of sLex display can be achieved, and STD-NMR studies surprisingly reveal that the mimetic does not compete with GDP-fucose at the enzymatic binding site.
Fucosyltransferase-specific inhibition via next generation of fucose mimetics / Martin K.C.; Tricomi J.; Corzana F.; Garcia-Garcia A.; Ceballos-Laita L.; Hicks T.; Monaco S.; Angulo J.; Hurtado-Guerrero R.; Richichi B.; Sackstein R.. - In: CHEMICAL COMMUNICATIONS. - ISSN 1359-7345. - ELETTRONICO. - 57:(2021), pp. 1145-1148. [10.1039/d0cc04847j]
Fucosyltransferase-specific inhibition via next generation of fucose mimetics
Tricomi J.;Richichi B.
;
2021
Abstract
The ability to custom-modify cell surface glycans holds great promise for treatment of a variety of diseases. We propose a glycomimetic ofl-fucose that markedly inhibits the creation of sLeXby FTVI and FTVII, but has no effect on creation of LeXby FTIX. Our findings thus indicate that selective suppression of sLex display can be achieved, and STD-NMR studies surprisingly reveal that the mimetic does not compete with GDP-fucose at the enzymatic binding site.
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