Mucin-type O-linked glycosylation is the most abundant form of O-linked glycosylation in higher eukaryotes. It begins with the addition of -N-acetyl-D-galactosamine to serine and threonine residues of membrane-bound and secreted proteins initiated by a family of polypeptide N-acetylgalactosamine transferases. After the addition of the GalNAc residue, various glycosyltransferases further elaborate to create large structures of carbohydrates. Misregulation of the various glycosyltransferases or changes in the downstream elaborations have ties to various diseases such as cancer, hematological disorders, and Wiskott-Aldrick syndrome. Currently there is no specific metabolic chemical reporter for mucin-type glycosylation. Here, we show the synthesis and characterization of 4FGalNAz and its potential in revealing more about this abundant form of glycosylation.

Fluorinated analog of metabolic chemical reporter N-azidoacetylgalactosamine demonstrates selectivity towards mucin-type O-linked glycosylation

ACS Spring Meeting 2021

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