Nisin
Lantibiotic peptide from Lactococcus lactis used as a food preservative, with unique lipid II targeting mechanism.
Chemical Identity
| Property | Value |
|---|---|
| Chemical Formula | C143H228N42O37S7 |
| Molecular Weight | 3354 Da |
| CAS Number | 1414-45-5 |
| Peptide Class | Lantibiotic (34 amino acids) |
| Lanthionine Bonds | 5 (3 lanthionine, 2 methyllanthionine) |
| Origin | Lactococcus lactis |
Structure
Nisin is a 34-amino acid lantibiotic containing five intramolecular thioether bridges (lanthionine and methyllanthionine) that create a rigid cage-like structure. The N-terminal domain contains three lanthionine bridges forming three interconnected rings (A, B, C), while the C-terminal domain has two methyllanthionine bridges (rings D, E).
Mechanism of Action
Nisin has a unique dual mechanism: (1) it binds lipid II, the essential peptidoglycan precursor, through its pyrophosphate cage, simultaneously inhibiting cell wall synthesis; (2) the lipid II-nisin complex oligomerizes to form large pores in the cytoplasmic membrane, causing rapid depolarization. This dual targeting makes resistance development very rare.
Clinical Applications
- Food preservation: GRAS status for dairy, meat, and beverages
- Anti-listerial: Particularly effective against Listeria monocytogenes
- Dairy industry: Prevention of clostridial spoilage
- Research: Model for lantibiotic engineering
- Therapeutic potential: Under investigation for clinical use
Pharmacology
- Spectrum: Broad gram-positive (including spore-formers)
- Potency: 1000x more active than many chemical preservatives
- Stability: Acid-stable, heat-stable
- pH range: Active at pH 2-7
References
- Delves-Broughton, J., et al. (1996). Nisin as a food preservative. Food Australia, 48, 80-85.
- Breukink, E., & de Kruijff, B. (1999). The lantibiotic nisin, a special case or not? Biochimica et Biophysica Acta, 1462, 223-234.
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