chemical properties
- molecular weight: typically >200 kDa, some exceeding several MDa
- structure: heavily glycosylated proteins with tandem repeat domains rich in serine, threonine, and proline
- types: secreted (e.g. MUC2, MUC5AC) and membrane-bound (e.g. MUC1, MUC4)
- solubility: hydrophilic; forms viscous gels in aqueous environments
usefulness in biology and medicine
- mucins protect epithelial surfaces by trapping dust, bacteria, and viruses in mucus layers.
- they facilitate smooth passage of materials (e.g., food, waste) through mucosal linings.
- altered mucin expression is associated with diseases like cystic fibrosis, chronic bronchitis, ulcerative colitis, and cancer.
- mucins serve as biomarkers in oncology; for example, overexpression of MUC1 is linked to breast and pancreatic cancer.
- synthetic mucin-like materials are being explored in drug delivery and tissue engineering.
- mucins trap and aggregate pathogens, preventing their attachment to epithelial cells.
- their glycan structures can bind to microbial surface proteins, neutralizing them or directing them for clearance.
- they support the activity of antimicrobial peptides and maintain microbiome balance.
- research highlights:
- bacteria:
- viruses:
research links