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LF f((1-16) - (17-48)) [id=LFB0008]

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

Gram-negative: Escherichia coli L361 (MIC=4 ÁM).

Description :
Production method: Chymosin hydrolysis and purification with LC method.

Length : 49 Mass (Da): 5 836.81 Common Amino Acids : R
Isolectric Point : 11.81 Net Charge : 10 Absent Amino Acids : DHY
Basic Residues : 12 Acidic Residues : 2 Hydrophobic Residues : 18
Polar Residues : 10 Boman Index : -119.42 Hydropathy Index : -0.508
Aliphatic Index : 61.84 Instability Index : 0 Extinction Coefficient : 22250
Absorbance 280nm : 463.54

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 activity in bovine lactoferrin-derived peptides

Cited Entries: LFB0008, LFB0013, LFB0014, LFB0017, LFB0087, LFB0091, LFB0093, LFB0119

Authors:Hoek, K.S., Milne, J.M., Grieve, P.A., Dionysius, D.A., Smith, R.
Journal: Antimicrobial Agents and Chemotherapy 1997, 41(1).
Abstract: Several peptides sharing high sequence homology with lactoferricin B (Lf-cin B) were generated from bovine lactoferrin (Lf) with recombinant chymosin. Two peptides were copurified, one identical to Lf-cin B and another differing from Lf-cin B by the inclusion of a C-terminal alanine (lactoferricin). Two other peptides were copurified from chymosin-hydrolyzed Lf, one differing from Lf-cin B by the inclusion of C-terminal alanyl-leucine and the other being a heterodimer linked by a disulfide bond. These peptides were isolated in a single step from chymosin-hydrolyzed Lf by membrane ion-exchange chromatography and were purified by reverse-phase high-pressure liquid chromatography (HPLC). They were characterized by N-terminal Edman sequencing, mass spectrometry, and antibacterial activity determination. Pure lactoferricin, prepared from pepsin-hydrolyzed Lf, was purified by standard chromatography techniques. This peptide was analyzed against a number of gram-positive and gram-negative bacteria before and after reduction of its disulfide bond or cleavage after its single methionine residue and was found to inhibit the growth of all the test bacteria at a concentration of 8 microM or less. Subfragments of lactoferricin were isolated from reduced and cleaved peptide by reverse-phase HPLC. Subfragment 1 (residues 1 to 10) was active against most of the test microorganisms at concentrations of 10 to 50 microM. Subfragment 2 (residues 11 to 26) was active against only a few microorganisms at concentrations up to 100 microM. These antibacterial studies indicate that the activity of lactoferricin is mainly, but not wholly, due to its N-terminal region.

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