LF f(18-42) modified [id=LFH0026]

Synonym: LF f(18-42) linear ; HLP-1

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

Gram-positive: Enterococcus faecalis 19433 (MIC=1250 然), Enterococcus faecium 6569 9(MIC=625 然), Lactobacillus lactis subsp. lactis 29146 (MIC=1250 然), Staphylococcus aureus oxford (MIC=1250 然), Staphylococcus aureus 700698 (MIC=1250 然).

Gram-negative: Escherichia coli serotype O111 8007 (MIC=2500 然), Klebsiella pneumoniae subsp. pneumoniae 49472 (MIC=1250 然), Acinetobacter sp. 14291 (MIC=625 然), Salmonella typhimurium 13311 (MIC=1250 然).

NOTE: No activity against Staphylococcus aureus ATCC 25923, Escherichia coli ATCC 25922 (>200 痢/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 (Citation: 1).
Nine peptides (LFH0002, LFH0003, LFH0016, LFH0045, LFH0056, LFH0057, LFH0058, LFH0059) derived from human lactoferricin are tested against a selection of Gram-positive and Gram-negative strains. Four of these peptides, LFH0003, LFH0016, LFH0026 and LFH0045, were active against all of the 9 bacterial strains examined, while LFH0002 and LFH0059 exhibited strain specific activity (Citation: 2).
Length : 25 Mass (Da): 3 022.28 Common Amino Acids : R
Isolectric Point : 11.58 Net Charge : 6 Absent Amino Acids : AEHLY
Basic Residues : 7 Acidic Residues : 1 Hydrophobic Residues : 5
Polar Residues : 7 Boman Index : -87.98 Hydropathy Index : -1.116
Aliphatic Index : 38.8 Instability Index : 0 Extinction Coefficient : 5625
Absorbance 280nm : 234.38

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)

 2 LFH0016  100.0%  -----------------TKCFQWQRN----------------------- 
 3 LFH0020   88.9%  -----------------TKCFQWQGN----------------------- 
 4 LFH0017   88.9%  -----------------TKCGQWQRN----------------------- 
 5 LFH0018   77.8%  -----------------TKCFGWGRN----------------------- 
 6 LFH0019   88.9%  -----------------TGCFQWQRN----------------------- 
 7 LFH0011  100.0%  -------------QPEATKCFQWQRNMRKVR------------------ 
 8 LFH0012  100.0%  --------------PEATKCFQWQRNMRKVR------------------ 
 9 LFH0013  100.0%  ---------------EATKCFQWQRNMRKVR------------------ 
10 LFH0014  100.0%  ----------------ATKCFQWQRNMRKVR------------------ 
11 LFH0041   91.7%  -------------------CFQWQRNMRKVA------------------ 
12 LFH0043  100.0%  --------------------FQWQRNMRK-------------------- 
13 LFH0040   91.7%  -------------------CFQWQRNMRKAR------------------ 
14 LFH0015  100.0%  -----------------TKCFQWQRNMRKVR------------------ 
15 LFH0038   91.7%  -------------------CFQWQRNMAKVR------------------ 
16 LFH0039   91.7%  -------------------CFQWQRNMRAVR------------------ 
17 LFH0021  100.0%  -----------------TKCFQWQRNMRKVR------------------ 
18 LFH0027  100.0%  ------------------KCFQWQRNMRKVR------------------ 
19 LFH0030   91.7%  -------------------AFQWQRNMRKVR------------------ 
20 LFH0044  100.0%  --------------------FQWQRNMRKV------------------- 
21 LFH0049  100.0%  --------------------FQWQRNMRKVR------------------ 
22 LFH0045  100.0%  --------------------FQWQRNMRKVR------------------ 
23 LFH0031   91.7%  -------------------CAQWQRNMRKVR------------------ 
24 LFH0055  100.0%  ---------------------QWQRNMRKVR------------------ 
25 LFH0022  100.0%  -----------------TKCFQWQRNMRKVRG----------------- 
26 LFH0029  100.0%  -------------------CFQWQRNMRKVR------------------ 
27 LFH0033   91.7%  -------------------CFQAQRNMRKVR------------------ 
28 LFH0056  100.0%  ------------------------RNMRKVR------------------ 
29 LFH0032   91.7%  -------------------CFAWQRNMRKVR------------------ 
30 LFH0034   91.7%  -------------------CFQWARNMRKVR------------------ 
31 LFH0023   93.3%  -----------------TKCFQWQWNMRKVRG----------------- 
32 LFH0057  100.0%  ---------------------------RKVR------------------ 
33 LFH0035   91.7%  -------------------CFQWQANMRKVR------------------ 
34 LFH0036   91.7%  -------------------CFQWQRAMRKVR------------------ 
35 LFH0046   90.9%  --------------------FQWQRNIRKVR------------------ 
36 LFH0047   90.9%  --------------------FQWQRNIRKVR------------------ 
37 LFH0048   90.9%  --------------------FQWQRNPRKVR------------------ 
38 LFH0037   91.7%  -------------------CFQWQRNARKVR------------------ 
39 LFH0024  100.0%  -----------------TKCFQWQRNMRKVRGPPVSCIKR--------- 
40 LFH0026  100.0%  -----------------TKCFQWQRNMRKVRGPPVSCIKRDS------- 
41 LFH0025  100.0%  -----------------TKCFQWQRNMRKVRGPPVSCIKRDS------- 
42 LFH0042  100.0%  -------------------CFQWQRNMRKVRGPPVSCI----------- 
43 LFH0054  100.0%  --------------------FQWQRNMRKVRGPPVS------------- 
44 LFH0028  100.0%  ------------------KCFQWQRNMRKVRGPPVSCI----------- 
46 LFH0058  100.0%  ---------------------------RKVRGPPVSCIKRDSP------ 
47 LFH0059  100.0%  ------------------------------------CIKRDSP------ 
48 LFH0009A 100.0%  GRRRRSVQWCA-------------------------------------- 
51 LFH0004  100.0%  GRRRRSVQWCA-------------------------------------- 
52 LFH0003  100.0%  GRRRRSVQW---------------------------------------- 
53 LFH0002  100.0%  GRRRRS------------------------------------------- 

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
Citation: 3

Factors contributing to the potency of antimicrobial cationic peptides from the N-terminal region of human lactoferrin

Cited Entries: LFH0002, LFH0003, LFH0016, LFH0017, LFH0018, LFH0019, LFH0020, LFH0026, LFH0045, LFH0056, LFH0057, LFH0058, LFH0059

Authors:Moriarty, L.C., Joannou, C.L., van den Berg, J.J.M., Gorinsky, B., Evans, R.W.
Journal: FEMS Microbiology Letters 2004, 239(2).
Abstract: This study investigated the antimicrobial activities of peptides derived from the N-terminal region of human lactoferrin, and examined the contributions of individual residues to the activity of the most potent peptide. Two regions of antimicrobial activity were identified, the first corresponding to a weakly active peptide, HLP-9, comprising residues 1-9, and a second corresponding to a more potent peptide, HLP-10, comprising residues 18-26 and containing the hexapeptide motif, FQWQRN. Inhibitory studies on peptides from the first region confirm the importance of tryptophan residues in enhancing and broadening peptide activity. Inhibitory studies with glycine-substituted homologues of the more potent peptide showed that F21/G and R25/G substitutions resulted in a major reduction or complete loss of activity, while increased peptide cationicity or flexibility had little effect. Our findings demonstrate that F21 and R25 are critical determinants of potency for HLP-10, and that the second aromatic residue may act synergistically with W23 in developing and enhancing the activity of this cationic peptide.
Keywords: Cationic antimicrobial peptides; Human lactoferrin peptide; Lactoferrin

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