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LF f(21-31) modified [id=LFH0091]

Synonym: LF12-C8

Producer Organism : Native Protein : Production Method :
Human Recombinant lactoferrin (rLF) Recombinant
Activity : Antibacterial
Target Organisms :

Gram-positive: Staphylococcus aureus ATCC 25923 (MIC=10 然 or MIC=19 然).

Gram-negative: Escherichia coli DC2 CGSC 7139 (MIC=2 然 or MIC=10 然).

Description :
All lipopeptides (LFH0090 - LFH0095) were more effective than the parent (LFH0045) or the recombinant peptide (LFH0096) against both Gram-negative and Gram-positive bacteria. It was found that 12 carbon units (LFH0092) constitute the optimal acyl chain length, enhancing the antibacterial activity and binding of lipopolysaccharide by up to two orders of magnitude (citation 1).
Length : 11 Mass (Da): 1 549.47 Common Amino Acids : R
Isolectric Point : 12.81 Net Charge : 4 Absent Amino Acids : ACDEGHILPSTY
Basic Residues : 4 Acidic Residues : 0 Hydrophobic Residues : 3
Polar Residues : 1 Boman Index : -56.33 Hydropathy Index : -1.809
Aliphatic Index : 26.36 Instability Index : 0 Extinction Coefficient : 5500
Absorbance 280nm : 550

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

Enhancement of antibacterial and lipopolysaccharide binding activities of a human lactoferrin peptide fragment by the addition of acyl chain

Cited Entries: LFH0045, LFH0090, LFH0091, LFH0092, LFH0093, LFH0094, LFH0095, LFH0096

Authors:Majerle, A., Kidric, J., Jerala, R.
Journal: Journal of Antimicrobial Chemotherapy 2003, 51(5).
Abstract: Cationic antibacterial peptides are potentially therapeutic in the treatment of sepsis, because of their amalgamated antibacterial and lipopolysaccharide-binding activities. We prepared acyl analogues of the peptide fragment of human lactoferrin, which originally had weak antibacterial activity. It was found that 12 carbon units constitute the optimal acyl chain length, enhancing the antibacterial activity and binding of lipopolysaccharide by up to two orders of magnitude. Lactoferrin-based lipopeptides approached the activity of polymyxin B, a lipopeptide of natural origin, but were also active against Gram-positive bacteria.

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