The sialic acids found on eukaryotic glycans have remarkably diverse core structures, with a range of modifications at C5, C7, C8 and C9. These carbohydrates have been found to play key roles in cell cell interactions within eukaryotes and often serve as the initial site of attachment for viruses and bacteria. Consequently simple changes to the structures of the sialic acids can result in profoundly different and often opposing biological effects. Of particular importance are modifications at the 8-position. These include O-acetylation, carried out by an acetyl transferase, and particularly polysialylation, catalyzed by a polysialyltransferase. As part of a structural and mechanistic study of sialyltransferases and polysialyl-transferases, access was needed to sialic acid-containing oligosaccharides that are modified at the 8-position of the sialic acid to render this center non-nucleophilic. The free 8-modified sialic acid analogues were synthesized using a concise, divergent chemical synthetic approach, and each was converted to its cytidine monophosphate (CMP) sugar donor form using a bacterial CMP-sialic acid synthetase. The transfer of each of the modified donors to lactose by each of two sialyltransferases was investigated, and kinetic parameters were determined. These yielded insights into the roles of interactions occurring at that position during enzymatic sialyl transfer. A transferase from Campylobacter jejuni was identified as the most suitable for the enzymatic coupling and utilized to synthesize the 8 ''-modifed sialyl lactose trisaccharides in multimilligram amounts.