MUCIN PEPTIDE MICROARRAYS IN STUDIES OF PROTEIN-CARBOHYDRATE BINDING EVENTS

摘要

Mucins are densely glycosylated proteins that populate the cell-surface of epithelial tissues [1]. The extracellular tandem repeat peptide regions rich on proline, threonine and serine residues characterize the mucins. By display of O-glycans often organized in a multivalent fashion, the mucins and mucin like glycoproteins are involved in a plethora of cell-surface binding events [2]. Glycans on mucins often act as ligands for invading pathogens, studies of such interactions are useful for characterization of microbes and viruses as well as to develop new anti-adhesive drugs. Mucins also play a critical role in cancer progression and through aberrant glycosylation tumor-cell adhesion and anti-adhesion events can be modulated. By chemical synthesis of well-defined glycan and glycopeptide probes we aim to identify and map the functions of mucins and their interacting binding partners involved in cancer and infection processes.