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LF f(17-31) modified [id=LFP0002]

Synonym: LFp W8

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

Gram-positive: Staphylococcus aureus ATCC 25923 (MIC=500 然 or MIC>500 然).

Gram-negative: Escherichia coli ATCC 25922 (MIC=219 然).

Description :
Production method: Synthetic.

Eighth residue replaced with tryptophan, doubling the antibacterial activity of LFP0001 against E. coli (Citation 1).
Length : 15 Mass (Da): 1 987.95 Common Amino Acids : R
Isolectric Point : 12.24 Net Charge : 5 Absent Amino Acids : ADEFGHLMVY
Basic Residues : 5 Acidic Residues : 0 Hydrophobic Residues : 3
Polar Residues : 4 Boman Index : -68.69 Hydropathy Index : -1.98
Aliphatic Index : 26 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.

Multiple Sequence Alignment (MSA)


1 LFPNATIVE 100.0%  SKCRQWQSKIRRTNPIFCIRR 

2 LFP0003   100.0%  -KCRQWQSKIRRTNPIFCIRR 

3 LFP0004   100.0%  ---RQWQSKIRR--------- 
4 LFP0005   100.0%  ---RQWQSKIRRT-------- 

5 LFP0001   100.0%  SKCRQWQSKIRRTNP------ 

6 LFP0002    93.3%  SKCRQWQWKIRRTNP------ 

Citation: 1

Antibacterial activity of 15-residue lactoferricin derivatives

Cited Entries: LFH0022, LFH0023, LFB0031, LFB0034, LFB0035, LFB0036, LFB0037, LFB0038, LFB0039, LFB0040, LFB0041, LFB0042, LFB0043, LFB0044, LFB0045, LFB0046, LFB0047, LAG0002, LAG0003, LFP0001, LFP0002, LFM0001, LFM0002

Authors:Str鷰, M.B., Svendsen, J.S., Rekdal, O.
Journal: The Journal of Peptide Research 2000, 56(5).
Abstract: Lactoferricins are a class of antibacterial peptides isolated after gastric-pepsin digest of the mammalian iron-chelating-protein lactoferrin. For investigation of antibacterial activity, we prepared short synthetic derivatives of bovine, human, caprine, murine and porcine lactoferricins with 15-amino-acid residues of high sequence homology. The peptides corresponded to amino-acid residues 1731 of the mature bovine lactoferrin. Only the bovine and caprine derivatives displayed measurable antibacterial activity, with the bovine one having a minimal inhibitory concentration of 24 痠 and being 10 times more active than the caprine one against Escherichia coli. An alanine-scan of the bovine lactoferricin derivative was performed to identify specific amino acids that were important for the antibacterial activity. We found that neither of the two tryptophan residues (Trp 6 and Trp 8) present in the bovine lactoferricin derivative could be replaced by alanine without a major loss of antibacterial activity. The other lactoferricin derivatives tested contained only one tryptophan residue (Trp 6). Modified human, caprine and porcine lactoferricin derivatives containing two tryptophan residues (Trp 6 and Trp 8) displayed minimal inhibitory concentrations of 74, 174 and 219 痠, respectively, which represented up to a six-fold increase in antibacterial activity. The alanine-scan also revealed that the antibacterial activity was increased when acetamidomethyl-protected cysteine and unprotected glutamine (Cys 3 and Gln 7) were replaced with alanine. Only the bovine lactoferricin derivative and a few of its alanine-modified derivatives displayed measurable activity against Staphylococcus aureus.
Keywords: alanine-scan; Antibacterial peptide; Lactoferricin; minimal inhibitory concentration; peptide modifications
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鷰, 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 structureactivity 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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