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LF f(18-37) [id=LFP0003]

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

Gram-positive: Staphylococcus aureus ATCC 25923 (MIC=32 g/ml).

Gram-negative: Escherichia coli ATCC 25922 (MIC=64 g/ml).

Yeast: Candida albicans ATCC 14053 (MIC=32 g/ml).

Description :
Production method: Synthetic.

In the 20-residue LFcin peptides, LFcin B-20 (LFB0095) was the most active against Gram-negative and Gram-positive bacteria and fungi. In addition, LFcin P-20 (LFP0003) also showed high growth-inhibitory activity against E. coli, S. aureus, and C. albicans when compared with LFcin H-20 (LFH0028). The nine-residue LFcin peptides (LFH0043, LFB0098, LFP0004) are less active than twenty-residue LFcin peptides (LFH0028, LFB0095, LFP0003) (Citation: 1).
Length : 20 Mass (Da): 2 590.80 Common Amino Acids : R
Isolectric Point : 12.34 Net Charge : 7 Absent Amino Acids : ADEGHLMVY
Basic Residues : 7 Acidic Residues : 0 Hydrophobic Residues : 5
Polar Residues : 5 Boman Index : -86.76 Hydropathy Index : -1.175
Aliphatic Index : 58.5 Instability Index : 0 Extinction Coefficient : 5625
Absorbance 280nm : 296.05

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

Synthetic porcine lactoferricin with a 20-residue peptide exhibits antimicrobial activity against Escherichia coli, Staphylococcus aureus, and Candida albicans

Cited Entries: LFH0028, LFH0043, LFB0095, LFB0098, LFP0003, LFP0004

Authors:Chen, H.-L., Yen, C.-C., Lu, C.-Y., Yu, C.-H., Chen, C.-M.
Journal: Journal of Agricultural and Food Chemistry 2006, 54(9).
CrossRef External Link
Abstract: Lactoferricins are positively charged, highly basic peptides that are generated upon gastric pepsin cleavage of various lactoferrins. In the past decade, there has been active investigation of the key antimicrobial segments of the various shorter synthetic bovine and human lactoferricins, but not in porcine lactoferricin. These studies have demonstrated the distinct solution structures of lactoferricin in bovine and human and established the multifunctional nature of the antibacterial, antifungal, antiendotoxin, and antiviral activities of lactoferricins. However, the protective effects of porcine lactoferricins have yet to be elucidated. In the present study, a series of synthetic derivatives of porcine, bovine, and human lactoferricins with 20-residue and 9-residue peptides were prepared to investigate their antimicrobial nature. We found that the 20-residue porcine lactoferricin (LFcin P-20) displayed antimicrobial activity against Escherichia coli ATCC25922, Staphylococcus aureus ATCC25923, and Candida albicans ATCC14053. The minimal inhibitory concentrations and minimal bactericidal concentrations of LFcin P-20 ranged from 12 to 25 μM when tested in bacteria and fungi. LFcin P-20 was 4 times more effective than human lactoferricin (LFcin H-20), but slightly less effective than bovine lactoferricin (LFcin B-20).
Keywords: Porcine lactoferricin; antimicrobial activity; synthetic peptide; minimal inhibitory concentration (MIC); minimal bactericidal concentration (MBC).

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