Epithelial tissues generate distinct types of mucus to provide a wide variety of biological functions such as tissue hydration, pathogen defense, and mediating absorption into the body. The major glycoprotein component of mucus, mucins, play a critical role in imparting the physicochemical properties necessary to support mucus biological functions. Mucin glycoproteins are characterized by a large, rod-like proline threonine serine (PTS) domain that contains a variable level of glycosylated threonine and serine residues. Changes to mucin structure and glycosylation patterns may alter mucus’s biological function and properties. In this work, we chemically synthesized a panel of mucin glycopolypeptides containing naturally and unnaturally occurring amino acids to investigate the structural and biological implications of these alterations. Carbohydrate chemistry, amino acid <i>N</i>-carboxyanhydride (NCA) polymerization, and protease degradation experiments were utilized during the course of this work.

Mucin analogs with tunable biodegradation

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