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Disulfide bridges in mucin polymers are covalent bonds formed between cysteine residues of mucin monomers, enabling the assembly of large, gel-forming glycoproteins that constitute the structural framework of mucus. These bridges are essential for both intra- and intermolecular stabilization and polymerization of mucins such as MUC2, MUC5AC, and MUC5B. The integrity and density of these disulfide-linked networks determine mucus viscosity and elasticity—key properties for effective barrier function and clearance mechanisms. Abnormalities in this cross-linking can lead to diseases characterized by defective mucus barriers or impaired clearance.
Disruption or modulation of disulfide bond formation to alter mucus properties.
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