Nisin
The food-grade antimicrobial peptide — a 34-amino-acid lantibiotic used in food preservation worldwide for 50+ years, with emerging pharmaceutical applications against MRSA and biofilms.
A 34-amino-acid polycyclic antimicrobial peptide produced by Lactococcus lactis, containing unusual lanthionine and methyl-lanthionine bridges, with a dual mechanism of lipid II binding and pore formation.
Mechanism of action
Dual mechanism: (1) Binds lipid II (the same peptidoglycan precursor target as vancomycin) with high affinity, sequestering it and blocking cell wall synthesis; (2) Uses the lipid II-nisin complex to form pores (2–2.5 nm diameter) in the bacterial membrane, causing rapid ion efflux and cell death. This dual action makes resistance development difficult. Active against gram-positive bacteria; gram-negatives are protected by the outer membrane.
Primary uses
- Food preservation (dairy, meat, beverages)
- Anti-MRSA research
- Anti-biofilm strategies
- Mastitis treatment research (veterinary)
Typical dosing
Food use: typically 1–25 ppm. Pharmaceutical dosing under investigation for topical and local applications.
Regulatory status
FDA GRAS (Generally Recognized as Safe) status as a food preservative (since 1988). Approved as food additive E234 in the EU. Not FDA-approved as a pharmaceutical drug, though pharmaceutical applications are in development.
References
- [review] Breukink E, de Kruijff B. "Lipid II as a target for antibiotics." Nat Rev Drug Discov, 2006;5:321-332.
- [review] Shin JM, et al. "Biomedical applications of nisin." J Appl Microbiol, 2016;120:1449-1465.
Related peptides
This entry is for educational purposes only and does not constitute medical advice. Dosing information reflects published regulatory or research data and is not a recommendation. Many compounds described here are not approved for human use in the United States. Consult a licensed medical professional before considering any peptide therapy.