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The Fascione Lab studies glycans at the interface between chemistry and biology- a field commonly termed ‘chemical glycobiology’. Our focus is on deciphering the roles that these biomolecules play in the etiology of disease, with the overall aim of developing chemical tools to study and perturb their activity in vivo.

Chemical glycobiology tools for sialic and

ulosonic acid sugars

Pse5Ac7Ac vs Neu5Ac

Developing novel chemical glycobiology tools for bacterial nonulosonic acid sugars such as Pseudaminic acid (Pse), the "evil twin" of human sialic acid (Neu5Ac). Including enzyme substrates, cellular probes and therapeutic inhibitors to dissect and perturb biosynthesis in bacteria.

Synthetic and mechanistic carbohydrate


Automated glycan assembly
Glycosyl oxathianes

Chemical synthesis of ulosonic and sialic acids and other complex glycans; methods and mechanistic exploration of stereoselective glycosylation; automated glycan assembly.

Chemical enzymology for synthesis and exploration using carbohydrate active enzymes

KpsS1 Pseudaminyltransferases
Reverse thiophosphorylases

Chemoenzymatic approaches for the synthesis of nonulosonic acid glycans; carbohydrate active enzyme discovery and characterisation; new modes of enzyme activity using unnatural substrates and sugars.

Protein bioconjugation for the development of (glyco)theranostics

OPAL bioconjugation
Protein glycoconjugation

Novel methods for the bio/glycoconjugation of proteins which can be applied in 'chemical glycomedicine' approaches for the prevention and treatment of disease.

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