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.
Tomita
M
M
Research Laboratory, Morinaga Milk Industry Co. Ltd., Kanagawa, Japan.
Takase
M
M
Bellamy
W
W
Shimamura
S
S
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000494:pharmacology*; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D007781:Lactoferrin / Q000737:chemistry / Q000494:pharmacology*; D008969:Molecular Sequence Data; D010455:Peptides; D013329:Structure-Activity Relationship
D000900:Anti-Bacterial Agents; D010455:Peptides; D007781:Lactoferrin