A review: The active peptide of lactoferrin

A potent antimicrobial peptide, ‘lactoferricin’, was found to be generated upon gastric pepsin cleavage of lactoferrin. The active peptide consists mainly of a loop of 18 amino acid residues, derived from the N-terminal region of the lactoferrin molecule. Like various other antimicrobial peptides that display membrane-disruptive properties, it contains a high proportion of basic amino acid residues. A physiologically diverse range of micro-organisms was tested and found to be susceptible to inhibition by this natural peptide including Gram-negative and Gram-positive bacteria, yeasts and filamentous fungi. Its antimicrobial effect against sensitive micro-organisms was lethal. Electron microscopy studies revealed that it induces a profound change in cell ultrastructural features and causes substantial cell damage in bacteria and fungi. These findings suggest the possibility that active peptides of lactoferrin may have a role in the host defense against microbial disease. If produced in substantial quantities in vivo such peptides could have important physiological significance, especially in nursing infants.