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Antibacterial peptides of bovine lactoferrin: purification and characterization

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Dionysius, D.A. and Milne, J.M. (1997) Antibacterial peptides of bovine lactoferrin: purification and characterization. Journal of Dairy Science, 80 (4). pp. 667-674. ISSN 0022-0302


Article Link: https://doi.org/10.3168/jds.S0022-0302(97)75985-X


Three peptides with antibacterial activity toward enterotoxigenic Escherichia coli have been purified from a pepsin digest of bovine lactoferrin. All peptides were cationic and originated from the N-terminus of the molecule in a region where a bactericidal peptide, lactoferricin B, had been previously identified. The most potent peptide, peptide I, was almost identical to lactoferricin B; the sequence corresponded to residues 17 to 42, and the molecular mass was 3195 as deter-mined by mass spectrometry. A second, less active peptide, peptide II, consisted of two sequences, residues 1 to 16 and 43 to 48 (molecular mass of 2673), linked by a single disulfide bond. The third peptide, peptide III, also a disulfide-linked heter-odimer, corresponded to residues 1 to 48 (molecular mass of 5851), cleaved between residues 42 and 43. Peptides I and II displayed antibacterial activity toward a number of pathogenic and food spoilage microorganisms, and peptide I inhibited the growth of Listeria monocytogenes at concentrations as low as 2 µM. Bacterial growth curves showed that bactericidal effects of peptides I and II were observable within 30 min of exposure. The results confirmed and extended those of earlier studies suggesting that the bactericidal domain of lactoferrin was localized in the N-terminus and did not involve iron-binding sites.

Item Type:Article
Keywords:lactoferrin; pepsin digest; antibacterial properties
Subjects:Science > Microbiology > Immunology
Science > Microbiology > Bacteria
Animal culture > Cattle > Dairy processing. Dairy products
Live Archive:27 Mar 2024 02:08
Last Modified:27 Mar 2024 02:08

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