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LF f(18-32) modified [id=LFH0089]

Synonym: LFh W8, Y13

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

Gram-negative: Escherichia coli ATCC 25922 (MIC=55 ÁM).

Gram-positive: Staphylococcus aureus ATCC 25923 (MIC=500 ÁM).

Description :
Production method: Synthetic.

Eighth residue replaced with tryptophan and thirteenth residue replaced with tyrosine
Length : 15 Mass (Da): 2 033.01 Common Amino Acids : KWRQ
Isolectric Point : 10.89 Net Charge : 4 Absent Amino Acids : ADEHILPSV
Basic Residues : 4 Acidic Residues : 0 Hydrophobic Residues : 3
Polar Residues : 5 Boman Index : -49.16 Hydropathy Index : -1.62
Aliphatic Index : 0 Instability Index : 0 Extinction Coefficient : 12490
Absorbance 280nm : 892.14

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

Prediction of antibiotic activity and synthesis of new pentadecapeptides based on lactoferricins

Cited Entries: LFB0031, LFB0034, LFB0035, LFB0036, LFB0037, LFB0038, LFB0039, LFB0040, LFB0041, LFB0042, LFB0043, LFB0044, LFB0045, LFB0046, LFB0047, LFB0048, LFB0049, LFB0050, LFB0051, LFB0052, LFB0168, LFB0169, LFB0170, LFB0171, LFB0172, LFM0001, LFM0002, LFM0003, LFM0004, LFM0005, LFM0006, LFM0007, LFM0008, LFM0009, LFM0010, LFM0011, LFM0012, LFM0013, LFM0014, LFM0015, LFM0016, LFM0017, LFM0018, LFM0019, LFH0022, LFH0023, LFH0089, LAG0002, LAG0003, LFP0001, LFP0002

Authors:Lejon, T., Stiberg, T., Str°m, M. B., Svendsen, J. S.
Journal: Journal of Peptide Science 2004, 10(6): 6.
CrossRef External Link
Abstract: The antibacterial activity against Escherichia coli and Staphylococcus aureus has been studied for a number of modified pentadecapeptides based on lactoferricins of different origin. The peptides were classified by multivariate methods and quantitative structureľactivity relationships (QSAR) were developed using theoretically derived variables for the amino acids. For the modified peptides based on bovine lactoferricin (LFB) a model was calculated and used for prediction of new peptides that were then tested for antibacterial activity in order to improve peptide activity and to check the validity of the model. Models were also calculated including lactoferricins of different origin. Theories of the mechanism of action of the peptides are briefly discussed.
Keywords: lactoferrin; lactoferricin; pentadecapeptides; antibacterial activity; QSAR; predictions

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