LF f(17-31) modified [id=LFB0168]

Synonym: LFB K 1

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

Gram-negative: Escherichia coli ATCC 25922 (MIC=30 ÁM).

Gram-positive: Staphylococcus aureus ATCC 25923 (MIC=50 ÁM).

Description :
First residue replaced with lysine.
Length : 15 Mass (Da): 1 975.83 Common Amino Acids : K
Isolectric Point : 12.28 Net Charge : 7 Absent Amino Acids : DEFHINPSTVY
Basic Residues : 7 Acidic Residues : 0 Hydrophobic Residues : 4
Polar Residues : 2 Boman Index : -56.54 Hydropathy Index : -1.653
Aliphatic Index : 32.67 Instability Index : 0 Extinction Coefficient : 11000
Absorbance 280nm : 785.71

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

Construction and synthesis of lactoferricin derivatives with enhanced antibacterial activity

Cited Entries: LFH0026, LFB0031, LFB0089, LFB0164, LFB0165, LFB0166, LFB0167, LFB0168, LFB0169, LFB0170, LFM0020, LAG0006

Authors:Rekdal, O., Andersen, J., Vorland, L.H., Svendsen, J.S.
Journal: Journal of Peptide Science 1999, 5(1): 32-45.
Abstract: A series of peptides derived from sequences from human, bovine, murine and caprine lactoferrin has been prepared and investigated for antibacterial effect. Among the four species investigated peptides based on the bovine sequence displayed significant activity. The bovine sequence, bovine lactoferricin, showed a MIC value of 30 μg/mL on E. coli and S. aureus, whereas the three other lactoferricins possessed MIC values above 200 μg/mL. Based on these findings, novel peptides with enhanced antibacterial activities, were prepared with sequences designed by molecular modelling and structure-activity studies.
Keywords: Lactoferricin; Antibacterial; sequence modification; Qsar; ACM,acetamidomethyl; LFB,bovine lactoferricin; LFH,human lactoferricin; LFC,caprine lactoferricin; LFM,murine lactoferricin; QSAR,quantitative structure activity relationship; PLS,projection to latent structures
Citation: 2

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

Go to top