Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add more filters










Database
Language
Publication year range
1.
Carbohydr Res ; 477: 11-19, 2019 May 15.
Article in English | MEDLINE | ID: mdl-30933786

ABSTRACT

Enzymatic degradation of locust bean gum provides a Manß(1 → 4)Man disaccharide, which may be converted into the core Manß(1 → 4)GlcNAc disaccharide unit of all N-glycans via conversion to a 2-iodo-glycosyl azide, and Lafont rearrangement. The Manß(1 → 4)GlcNAc disaccharide may be used as a key intermediate for elaboration into more complex N-glycan structures providing a route to N-glycan oxazolines as donor substrates for ENGase enzymes that is considerably shorter than those reported previously.


Subject(s)
Galactans/metabolism , Mannans/metabolism , Oxazoles/metabolism , Plant Gums/metabolism , Polygalacturonase/metabolism , Polysaccharides/metabolism , Carbohydrate Conformation , Galactans/chemistry , Mannans/chemistry , Oxazoles/chemistry , Plant Gums/chemistry , Polysaccharides/chemistry
2.
Chem Commun (Camb) ; 55(36): 5287-5290, 2019 May 08.
Article in English | MEDLINE | ID: mdl-30994122

ABSTRACT

N-Azidoacetyl-d-glucosamine (GlcNAz) is a particularly useful tool in chemical biology as the azide is a metabolically stable yet accessible handle within biological systems. Herein, we report a practical synthesis of FmocAsn(N-Ac3GlcNAz)OH, a building block for solid phase peptide synthesis (SPPS). Protecting group manipulations are minimised by taking advantage of the inherent chemoselectivity of phosphine-mediated azide reduction, and the resulting glycosyl amine is employed directly in the opening of Fmoc protected aspartic anhydride. We show potential application of the building block by establishing it as a substrate for enzymatic glycan extension using sugar oxazolines of varying size and biological significance with several endo-ß-N-acetylglucosaminidases (ENGases). The added steric bulk resulting from incorporation of the azide is shown to have no or a minor impact on the yield of enzymatic glycan extension.


Subject(s)
Asparagine/chemical synthesis , Asparagine/metabolism , Glucosamine/chemical synthesis , Polysaccharides/chemistry , Acetylglucosaminidase/metabolism , Amino Acid Sequence , Amino Acids/chemistry , Azides/chemistry , Glucosamine/metabolism , Molecular Structure , Oxidation-Reduction , Solid-Phase Synthesis Techniques/methods , Structure-Activity Relationship
SELECTION OF CITATIONS
SEARCH DETAIL
...