LF f((1-16) - (43-48)) (S-S (9-45)) [id=LFB0009]

Synonym: Peptide II

Producer Organism : Native Protein : Production Method :
Cow Lactoferrin (LF) Enzymatic hydrolysis and Purification with LC method
Activity : Antibacterial
Target Organisms :

Gram-positive: Bacillus cereus ACM 446 (MIC=150 然), Listeria monocytogenes NCTC 7973 (MIC=75 然), Staphylococcus aureus NCTC 6571 (MIC=150 然).

Gram-negative: Escherichia coli strain 1 (MIC=75 然), Pseudomonas fluorescens wild strain (MIC=150 然), Salmonella salford IMVS 1710 (MIC=75 然).

Description :
Production method: Porcin pepsin hydrolysis and purification with LC method.

LFB0009 contained a sequence that has not previously been reported to be part of the bactericidal domain of bovine Lf (LFB0084). This peptide flanked the active loop region of LFB0092 and, although not as potent (or as basic) as LFB0092, LFB0009 clearly demonstrated a bactericidal effect toward E. coli (Citation: 1).
Length : 23 Mass (Da): 2 657.50 Common Amino Acids : R
Isolectric Point : 8.83 Net Charge : 2 Absent Amino Acids : DFGHMY
Basic Residues : 4 Acidic Residues : 2 Hydrophobic Residues : 8
Polar Residues : 5 Boman Index : -52.44 Hydropathy Index : -0.535
Aliphatic Index : 72.17 Instability Index : 0 Extinction Coefficient : 11125
Absorbance 280nm : 505.68

Wheel representation

Hydrophobicity plot

Red solid plot : values according to the hydrophobicity scale of Kyte and Doolittle (reference paper).
Yellow dashed plot : Experimentally determined hydrophobicity scale for proteins at membrane interfaces(reference paper).
Green dotted-dashed plot : prediction of transmembrane helices (reference paper). In this scale (unlike the others), more negative values reflect greater hydrophobicity.

Citation: 1

Antibacterial peptides of bovine lactoferrin: purification and characterization

Cited Entries: LFB0009, LFB0012, LFB0092

Authors:Dionysius, D.A., Milne, J.M.
Journal: Journal of Dairy Science 1997, 80(4).
CrossRef External Link
Abstract: 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 然. 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.
Keywords: Lactoferrin; pepsin digest; Antibacterial peptides

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