LF f(20-29) [id=LFP0005]

Producer Organism : Native Protein : Production Method :
Porcin Lactoferrin (LF) Synthetic
Activity : No activity detected
Target Organisms :

NOTE: No activity against Escherichia coli ATCC 25922, Escherichia coli wild strain, Staphylococcus aureus ATCC 25923, Enterococcus faecalis ATCC 29212 (>300 ÁM) .

Description :
Production method: Synthetic.

Lactoferricin analogs bLf 20-29 (LFB0108), caprine lactoferricin 20-29 (LAG0007), murine lactoferricin 20-29 (LFM0021), porcine lactoferricin 20-29 (LFP0005), and human lactoferricin 21-30 (LFH0044) were commercially synthesized and tested for their antibacterial activity. Among these peptides, bLf 20-29 was the most active against gram-positive and gram-negative bacteria and among analogs, only clf had measurable MIC values against E coli and S aureus (Citation: 1).
Length : 10 Mass (Da): 1 359.19 Common Amino Acids : R
Isolectric Point : 12.81 Net Charge : 4 Absent Amino Acids : ACDEFGHLMNPVY
Basic Residues : 4 Acidic Residues : 0 Hydrophobic Residues : 2
Polar Residues : 2 Boman Index : -60.11 Hydropathy Index : -2.23
Aliphatic Index : 39 Instability Index : 0 Extinction Coefficient : 5500
Absorbance 280nm : 611.11

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)



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 short hydrophobic and basic-rich peptides

Cited Entries: LFH0044, LFB0108, LAG0007, LFP0005, LFM0021

Authors:Chen, P.-W., Shyu, C.-L., Mao, F.C.
Journal: American Journal of Veterinary Research 2003, 64(9).
Abstract: OBJECTIVE-To design short and potent analogs of bovine lactoferricin by use of the concepts of lipophilic bulk and cationic charge. SAMPLE POPULATION-5 synthetic peptides of bovine lactoferricin. PROCEDURE: Antibacterial peptides were constructed by synthesizing several decapeptides rich in arginine and tryptophan. Basic residues of bovine lactoferricin (bLf 20-29; residues 20 to 29) were modified by substitution with arginine or lysine and nonbasic residues were modified by substitution with tryptophan, phenylalanine, or isoleucine. Synthetic peptides of bovine lactoferrin (LFB) were designated as LFB-RW (RRWWWRWRRW), LFB-KW (KKWWWKWKKW), LFB-RWa (RRWWRRWRRW), LFB-RF (RRFFFRFRRF), and LFB-RI (RRIIIRWRRI), where R, K, W, F, and I stand for arginine, lysine, tryptophan, phenylalanine, and isoleucine, respectively. Peptides were evaluated by determining their minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) against Escherichia coli, Staphylococcus aureus, and Enterococcus faecalis. RESULTS: LFB-RW, LFB-KW, and LFB-RWa possessed equivalent potency as bLf 20-29 against E coli. LFB-RW and LFB-RWa had a 2-fold increase in growth-inhibitory and bactericidal activity against S aureus, compared with bLf 20-29. LFB-RI had the lowest MIC value against E coli among the peptides but lost bactericidal activity. LFB-RW and LFB-KW had stronger bactericidal activities against S aureus or E faecalis, respectively, as well as E coli than the other synthetic peptides. LFB-RF also had antibacterial activity, but this was 2-fold less than that of LFB-RW, as determined by MIC and MBC values. CONCLUSIONS AND CLINICAL RELEVANCE: In construction of potent antibacterial peptides, inclusion of arginine, lysine, tryptophan, or isoleucine residues enhances effectiveness against certain bacteria, as measured by MIC or MBC values.

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