Lactoferrin—a multifunctional protein with antimicrobial properties

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Abstract

Lactoferrin is a member of the transferrin family of iron-binding proteins. Numerous functions have been reported and continue to be reported for the protein, some of which are related to its iron-binding properties. Its extensive antimicrobial activities were originally attributed to its ability to sequester essential iron, however, it is now established that it possesses bactericidal activities as a result of a direct interaction between the protein or lactoferrin-derived peptides. This article reviews the antimicrobial activities of lactoferrin and discusses the potential mode of action of lactoferrin-derived cationic peptides against Gram-negative bacteria in the light of recent studies.

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The role of cationic antimicrobial peptides in innate host defences.

Robert Hancock, Gill Diamond (2000)

Cationic antimicrobial peptides are found in all living species. A single animal can contain >24 different antimicrobial peptides, which fall into four structural classes. These peptides are produced in large quantities at sites of infection and/or inflammation and can have broad-spectrum antibacterial, antifungal, antiviral, antiprotozoan and antisepsis properties. In addition, they interact directly with host cells to modulate the inflammatory process and innate defences.

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Peptide antibiotics.

R. Hancock (1997)

The era of the "classical antibiotic" may be over. The emergence of resistance has seen to that. Yet no truly novel class of antibacterial agent has come on the market in the past 30 years. Currently there is great interest in peptide antibiotics, especially the cationic peptides. Thousands of such molecules have been synthesised and just a few are entering clinical trials. Because they kill bacteria quickly by the physical disruption of cell membranes, peptide antibiotics may not face the rapid emergence of resistance.