LF f(17-28) modified [id=LFB0179]

Producer Organism : Native Protein : Production Method :
Cow Lactoferrin (LF) Synthetic
Activity : Antibacterial
Target Organisms :

Gram-positive: Staphylococcus aureus JCM2151 (MIC=6 µM).

Gram-negative: Escherichia coli IID861 (MIC=6 µM).

Description :
Peptide with blocked cysteines
Length : Mass (Da): 0.00 Common Amino Acids :
Isolectric Point : Net Charge : Absent Amino Acids :
Basic Residues : 6 Acidic Residues : 0 Hydrophobic Residues : 3
Polar Residues : 1 Boman Index : Hydropathy Index :
Aliphatic Index : Instability Index : Extinction Coefficient :
Absorbance 280nm :

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

A review: The active peptide of lactoferrin

Cited Entries: LFH0024, LFB0084, LFB0089, LFB0097, LFB0178, LFB0179

Authors:Tomita, M., Takase, M., Bellamy, W., Shimamura, S.
Journal: Acta Paediatrica Japonica 1994, 36.
Abstract: 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.
Keywords: antimicrobial peptide, lactofemcin, lactoferrin, pepsin digestion.

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