Tess Baker

• Development of a Stereodivergent Route to Glycosylated Amino Acids
• MChem with Honours in Medicinal Chemistry

Glycosylation is the covalent attachment of a sugar molecule to a lipid or protein, typically occurring through a nitrogen or oxygen atom. Despite its crucial role in biological systems, protein glycosylation remains poorly understood.

Research by the McAllister Group investigated a synthesis route for producing O-glycosylated amino acids. They examined how reaction time influences the stereochemistry of the glycosidic bond, resulting in either an alpha or beta linkage between the sugar and amino acid. Expanding on this, I investigated how altering the stereochemistry of the starting amino acid affects this synthetic route. I synthesised both L and D isomers of Fmoc Serine Methyl Ester and Fmoc Threonine Methyl Ester for use in glycosylation reactions. Analytical methods including NMR and LCMS were used to determine the stereochemistry of the final glycosylated products, finding the initial stereochemistry of the amino acid did not affect the glycosidic bond’s orientation, but reaction time did.