Lactoferricin is a 25-amino-acid antimicrobial peptide (f17-41 of bovine lactoferrin; MW ~3126 g/mol for bovine form) generated by pepsin digestion of lactoferrin. Bovine lactoferricin (LfcinB) is substantially more antimicrobially active than the parent protein and exhibits broad-spectrum activity against bacteria, fungi, viruses, and parasites. It also demonstrates anticancer properties in preclinical models. It remains a preclinical research molecule with no approved therapeutic applications.
Category: Antimicrobial / Immune. Evidence rating: D (animal/preclinical only).
Clinical status: Preclinical research only. No clinical trials registered for lactoferricin as a standalone therapeutic.
Lactoferricin is a cationic amphipathic peptide derived from the N-terminal region of lactoferrin. The bovine form (LfcinB, residues 17-41: FKCRRWQWRMKKLGAPSITCVRRAF) adopts a cyclic structure via a disulfide bond between Cys19 and Cys36 of the parent protein. Its antimicrobial activity depends on…
Safety considerations: No human clinical trials have been conducted; Bovine lactoferricin is a natural product of lactoferrin digestion in the stomach; Potential for allergic reactions in individuals with cow milk protein allergy.
Reviewed by the PeptideAtlas Editorial Team. Last reviewed: 2026-08-12.
Related peptides: LL-37, Beta-Defensins, Alpha-Defensins.
Compare: Lactoferricin vs LL-37, Lactoferricin vs Beta-Defensins, Lactoferricin vs Alpha-Defensins.
No. Lactoferricin is a 25-amino-acid peptide fragment produced by pepsin digestion of lactoferrin, a much larger 80 kDa iron-binding glycoprotein found in milk and other secretions. Lactoferricin is more antimicrobially potent than intact lactoferrin.
Lactoferricin is generated naturally when lactoferrin is digested by pepsin in the stomach. Consuming lactoferrin supplements or dairy products would produce some lactoferricin during digestion, but the amount and bioavailability of active peptide are uncertain.
Bovine lactoferricin (LfcinB) has a more amphipathic structure with higher net positive charge than the human form (LfcinH), resulting in stronger electrostatic interaction with bacterial membranes. LfcinB also contains more tryptophan residues that facilitate membrane insertion.