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Evidence: MediumPeptide Research Only Immune & Anti-Inflammatory

Lactoferricin

also known as: Lactoferricin B, LfcinB, Lactoferricin H

An antimicrobial peptide from mother's milk — a potent cationic fragment of lactoferrin with broad-spectrum activity against bacteria, fungi, viruses, and parasites, plus emerging anticancer properties.

A 25-amino-acid (bovine) or 47-amino-acid (human) cationic peptide liberated from the N-terminal domain of lactoferrin during gastric digestion, with antimicrobial activity exceeding that of the parent protein.

Mechanism of action

Binds bacterial LPS and lipoteichoic acid via electrostatic interactions between cationic residues and anionic membrane components. Inserts into microbial membranes causing permeabilization. Also inhibits biofilm formation, has direct antiviral activity (binds viral surface glycoproteins), and shows anticancer activity via mitochondrial membrane disruption in tumor cells while sparing normal cells.

Primary uses

  • Antimicrobial peptide research
  • Anti-biofilm strategies
  • Food preservation research
  • Anticancer peptide development

Typical dosing

Not established

Research reagent. No established therapeutic dosing.

Regulatory status

Not approved as a therapeutic. Active area of research for antimicrobial peptide drug development and food safety applications.

Status as of this entry's last review, October 4, 2026. Approvals, compounding rules and sport rules change; the regulatory tracker is checked more often.

What the studies show

Lactoferricin is the antimicrobial peptide released when stomach pepsin cuts the milk protein lactoferrin. The studies below are laboratory work; none gives it to people. A 2026 study that resurrected ancestral lactoferrins found the peptide's membrane-breaking residues accumulated over mammalian evolution; it is in the References, as its title names lactoferrin rather than lactoferricin.

Review · 2005

What it does

Pepsin releases lactoferricin from lactoferrin under acidic conditions, as happens in the stomach. It keeps, and often exceeds, the parent protein's activities: strong antimicrobial, weaker antiviral, and antitumour and immune effects in laboratory studies.

PMID 16261252

In Vitro · 2026

Shorter versions

Full-length bovine lactoferricin and three truncated versions (15, 9 and 6 residues) were made and compared by structure and antibacterial activity; the truncations kept only part of the full peptide's effect.

PMID 42499550

References

  1. [review] Gifford JL, et al. "Lactoferricin: a lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties." Cell Mol Life Sci, 2005;62:2588-2598. PMID: 16261252.
  2. [pubmed] Sil T, et al. "Retracing the origin and evolution of a cryptic antimicrobial peptide within mammalian lactoferrin." PLoS Biol, 2026;24(8):e3003932. PMID: 42640877.
  3. [pubmed] Pei J, et al. "Conformational plasticity and truncational effects on bovine lactoferricin: structural determinants of enhanced antimicrobial activity." Front Cell Infect Microbiol, 2026;16:1888171. PMID: 42499550.

Related peptides

LL-37

The only human cathelicidin — an antimicrobial peptide with direct activity against bacteria, fungi, viruses, and biofilms, with additional roles in wound healing and immune signaling.

Pexiganan

A synthetic 22-amino-acid analogue of the frog-skin peptide magainin 2, tested as a 1% cream against oral ofloxacin in two phase 3 trials in 835 people with mildly infected diabetic foot ulcers; about 85-90% improved on either. Never approved.

Omiganan

An indolicidin-derived cationic antimicrobial peptide developed as a topical gel over two decades. Its catheter-infection phase 3 trials (completed 2003, and CLIRS, 2005–2008) missed their primary endpoints, and its 2015–2017 rosacea phase 3 programme produced one positive and one negative trial. Never approved.

HNP-1

The prototype human α-defensin — isolated from neutrophil granules by Ganz, Selsted and Lehrer in 1985; the dominant antimicrobial peptide in human neutrophils and a workhorse molecule of innate immunity. Research peptide only: no defensin has ever been developed as an approved drug.

Guides & tools

Disclaimer

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.