Chemically tunable mucin chimeras assembled on living cells

Significance Mucins are a diverse and heterogeneous family of glycoproteins that have been implicated in immunity and cancer. This work establishes a rapid and scalable route to synthetic mucin constructs with precisely defined glycan densities and chain lengths. Physical characterization indicates that the constructs both chemically and structurally emulate biological mucins and that dense mucin-type O-glycosylation imparts a remarkable degree of rigidity to the peptide backbone. Dual end-functionalized mucins were covalently conjugated to an engineered membrane protein on live mammalian cells. This strategy allows systematic variation in display of cell surface mucins with numerous applications in understanding the many biological roles of this unusual glycoprotein family.