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LF f(17-41) [id=LFM0020]

Synonym: Linear LfcinM

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

NOTE: No activity against Escherichia coli ATCC 25922, Staphylococcus aureus ATCC 25923 (>200 g/ml) .

Description :
Production method: Synthetic.

Peptide with blocked cysteines.
The cyclic bovin lactoferricin (LFB0086) and the linear lactoferricins of bovine (LFB0089), human (LFH0026), murine (LFM0020)and caprine (LAG0006) origin were synthesized and analyzed by mass spectrometry. Only Lf-cinB (LFB0086 and LFB0089) showed significant antibacterial activity against E. coli and S. aureus.
Length : 24 Mass (Da): 2 686.62 Common Amino Acids : K
Isolectric Point : 11.22 Net Charge : 5 Absent Amino Acids : ADFHITY
Basic Residues : 6 Acidic Residues : 2 Hydrophobic Residues : 5
Polar Residues : 8 Boman Index : -54.53 Hydropathy Index : -0.933
Aliphatic Index : 56.67 Instability Index : 0 Extinction Coefficient : 5500
Absorbance 280nm : 239.13

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 LFM0020 100.0%  EKCLRWQNEMRKVGGPPLSCVKKSS 
 2 LFM0013  80.0%  EKCLRWQWAMRKYGG---------- 
 3 LFM0016  80.0%  EKCLRWQWRMRKYGG---------- 
 4 LFM0018  73.3%  RKCLRWQWAMRKYGG---------- 
 5 LFM0019  73.3%  RKCLRWQWRMRKYGG---------- 
 6 LFM0003  86.7%  EKCLRWQWEMRKYGG---------- 
 7 LFM0015  80.0%  RKCLRWQWEMRKYGG---------- 
 8 LFM0012  80.0%  AKCLRWQWEMRKYGG---------- 
 9 LFM0014  73.3%  AKCLRWQWAMRKYGG---------- 
10 LFM0017  73.3%  AKCLRWQWRMRKYGG---------- 
11 LFM0005  86.7%  EKCLRWQWAMRKVGG---------- 
12 LFM0008  86.7%  EKCLRWQWRMRKVGG---------- 
13 LFM0010  80.0%  RKCLRWQWAMRKVGG---------- 
14 LFM0011  80.0%  RKCLRWQWRMRKVGG---------- 
15 LFM0006  80.0%  AKCLRWQWAMRKVGG---------- 
16 LFM0009  80.0%  AKCLRWQWRMRKVGG---------- 
17 LFM0004  86.7%  AKCLRWQWEMRKVGG---------- 
18 LFM0007  86.7%  RKCLRWQWEMRKVGG---------- 
19 LFM0021 100.0%  ---LRWQNEMRKV------------ 
20 LFM0001 100.0%  EKCLRWQNEMRKVGG---------- 
21 LFM0002  93.3%  EKCLRWQWEMRKVGG---------- 

Citation: 1

Lactoferricin of bovine origin is more active than lactoferricins of human, murine and caprine origin

Cited Entries: LFH0026, LFB0086, LFB0089, LAG0006, LFM0020

Authors:Vorland, L.H., Ulvatne, H., Andersen, J., Haukland, H.H., Rekdal, ., Svendsen, J.S., Gutteberg, T.J.
Journal: Scandinavian Journal of Infectious Diseases 1998, 30.
Abstract: The antimicrobial peptide lactoferricin is generated by gastric pepsin cleavage of lactoferrin. We have examined the antimicrobial activity of lactoferricins derived from lactoferrin of human, murine, caprine and bovine origin with minimal inhibitory concentration (MIC) and minimal bactericidal concentration (MBC) against E. coli ATCC 25922 and S. aureus ATCC 25923. We found that lactoferricin of bovine origin (Lf-cin B) was the most efficacious of the lactoferricins tested. By comparing the linear and cyclic Lf-cin B we found the cyclic peptide to be the most active. Lactoferricin B was moderately active against E. coli ATCC 25922 and S. aureus ATCC 25923, but had no activity against P. mirabilis or Y. enterocolitica. Lf-cin B showed good activity against C. albicans, C. tropicalis and C. neoformans.
Keywords: PEPTIDE antibiotics; Lactoferrin
Citation: 2

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

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