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LF f(21-31) [id=LFH0045]

Synonym: HLT2 ; HLP2 ; HLP-2

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

Gram-positive: Active against Staphylococcus aureus CCUG 1800 at 25 g/ml. Enterococcus faecalis 19433 (MIC=1250 M), Enterococcus faecium 6569 (MIC=967 M), Lactobacillus lactis subsp. lactis 29146 (MIC=312 M), Staphylococcus aureus oxford (MIC=1250 M), Staphylococcus aureus 700698 (MIC=1250 M), Staphylococcus aureus NCTC 10571 (MIC=14 M), Staphylococcus aureus ATCC 25923 (MIC=200 M or MIC>600 M).

Gram-negative: Active against Escherichia coli ML35 (no MIC), Escherichia coli serotype O111 NCTC 8007 (MIC=290-1250 M), Klebsiella pneumoniae subsp. pneumoniae 49472 (MIC=1250 M), Acinetobacter sp. 1421 (MIC=312 M), Salmonella typhimurium 13311 (MIC=312 M), Escherichia coli NCTC 10418 (MIC=579 M), Enterobacter aerogenes (MIC=290 M), Klebsiella sp. strain 3105 (MIC=290 M), Acinetobacter sp. (MIC=0.86 M), Escherichia coli wild type strain W3110 (MIC=80 M), Escherichia coli DC2 CGSC 7139 (MIC=40 M or MIC=200 M).

Filamentous fungi: Aspergillus fumigatus (EC50=142 M).

NOTE: No activity against Enterococcus faecalis ATCC 19433, Pseudomonas aeruginosa CCUG 551, Staphylococcus aureus MRS 3526 at 25 g/ml,Escherichia coli O6K5, Escherichia coli O14, Candida albicans ATCC 64549 at 10 g/ml,Providencia stuartii, Proteus mirabilis (>1000 M), Pseudomonas aeruginosa ATCC 27853 (>2000 M) .

Description :
Production method: Synthetic.

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: 6).
In order to find an optimal peptide length within the peptide sequence 1431 (LFH0011) with regard to antimicrobial activity, amino acid residues were removed one by one, starting from the N-terminal end. The most active peptides were the ones corresponding to residues LFH0014, LFH0021, LFH0027, and LFH0030. The trends of increasing antimicrobial activity from sequence 1431 (LFH0011) to 1731 (LFH0014) and decreasing from sequence 2031 (LFH0029) to 2231 (LFH0055) were statistically significant (Citation : 5).
Antibacterial activities for the linear (LFH0045) and the branched, dimeric (LFH0050), tetrameric (LFH0051), octameric (LFH0052) and hexadecemeric (LFH0053) MAPs were tested against P.aeruginosa. LFH0051, LFH0052 and LFH0053 exhibited strong antibacterial activity while LFH0045 and LFH0050 did not, up to a peptide concentration of about 200 mm. The peptide with the highest antibacterial activity was LFH0053 (Citation: 7).
LFH0054, corresponding to the loop region of human lactoferricin (LFH0009), LFH0045, corresponding to the positively charged portion of the loop region and LFH0079, corresponding to the uncharged portion of the loop region were synthetised and tested for their antimicrobial activity. LFH0054 and LFH0045 exhibited potent anti-bacterial activity against E. coli whereas LFH0079 had no activity (Citation: 2).
The difference between the activities of LFH0054 and LFH0045 against S. aureus could be explained by differences in peptide size, allowing uptake of HLP 2 rather than HLP 1, but it is more likely to be due to differences in flexibility and conformation if the peptide binds to the peptidoglycan. This would also explain why LFH0048 still has activity against S. aureus (Citation: 1).
In the presence of LPS, LFH0045 and LFH0048 were found to bind and adopt a beta-strand conformation rather than an alpha-helix. Furthermore, there is a time-dependent association of peptide that results in an ordered formation of peptide aggregates. The rate of interpeptide association was far greater in LFH0045-LPS than in LFH0048-LPS, which was consistent with the lag phase observed on the killing curves. These results allow us to propose a mechanism by which LFH0045 folds and self-assembles at the outer membrane surface before exerting its activity (Citation: 3).
LFH0045 was found to act at the cell membrane, causing complete loss of membrane potential after 10 min and of membrane integrity within 30 min, with irreversible damage to the cell as shown by rapid loss of viability. It causes membrane disruption of the outer membrane, resulting in lysis, and that structural considerations are important for antibacterial activity (Citation: 1).

Both 3D models for LFH0045 and LFb0109 showed that the beta-strand is centred between the aromatic residues giving both side chains the same orientations. The displacement towards the N-terminus observed for the b-strand in LFH0045, compared with its central location in LFB0109, could be less favourable to membrane interaction and therefore responsible for the decrease in activity. Such a model suggests for LFH0009 a mechanism similar to the one observed for LFB0086, where the absence of long-range interaction, present in lactoferrin, destabilises the first alpha helix, as observed in solution and, upon interaction with the membrane, could result in the formation of a beta-strand, as observed in the presence of LPS. The location of the beta-strand in relation to the positive charges, seems to define the efficiency of the activity of the peptide and may explain the difference in activity obtained between both peptides (Citation 4).
Length : 11 Mass (Da): 1 549.47 Common Amino Acids : R
Isolectric Point : 12.81 Net Charge : 4 Absent Amino Acids : ACDEGHILPSTY
Basic Residues : 4 Acidic Residues : 0 Hydrophobic Residues : 3
Polar Residues : 1 Boman Index : -56.33 Hydropathy Index : -1.809
Aliphatic Index : 26.36 Instability Index : 0 Extinction Coefficient : 5500
Absorbance 280nm : 550

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 LFH0010  100.0%  GRRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQA 
 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----------- 
45 LFH0007  100.0%  GRRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCI-- 
46 LFH0058  100.0%  ---------------------------RKVRGPPVSCIKRDSP------ 
47 LFH0059  100.0%  ------------------------------------CIKRDSP------ 
48 LFH0009A 100.0%  GRRRRSVQWCA-------------------------------------- 
49 LFH0009B 100.0%  -----------VSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCI-- 
50 LFH0005  100.0%  GRRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCI-- 
51 LFH0004  100.0%  GRRRRSVQWCA-------------------------------------- 
52 LFH0003  100.0%  GRRRRSVQW---------------------------------------- 
53 LFH0002  100.0%  GRRRRS------------------------------------------- 
54 LFH0006   97.9%  GRRRRSVQWCAVSQPEATKCFQWQRNMRRVRGPPVSCIKRDSPIQCI-- 

Citation: 1

Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherichia coli Serotype O111

Cited Entries: LFH0045, LFH0048, LFH0049, LFH0054

Authors:Chapple, D.S., Mason, D.J., Joannou, C.L., Odell, E.W., Gant, V., Evans, R.W.
Journal: Infection and Immunity 1998, 66(6).
Abstract: Lactoferricin includes an 11-amino-acid amphipathic alpha-helical region which is exhibited on the outer surface of the amino-terminal lobe of lactoferrin. Synthetic peptides homologous to this region exhibited potent antibacterial activity against a selected range of both gram-negative and gram-positive bacteria. An analog synthesized with methionine substituted for proline at position 26, which is predicted to disrupt the helical region, abolished antibacterial activity against Escherichia coli and considerably reduced antibacterial activity against Staphylococcus aureus and an Acinetobacter strain. The mode of action of human lactoferrin peptide (HLP) 2 against E. coli serotype O111 (NCTC 8007) was established by using flow cytometry, surface plasmon resonance, and transmission electron microscopy. Flow cytometry was used to monitor membrane potential, membrane integrity, and metabolic processes by using the fluorescent probes bis-1,3-(dibutylbarbituric acid)-trimethine oxonol, propidium iodide, and carbonyl cyanide m-chlorophenylhydrazone, respectively. HLP 2 was found to act at the cell membrane, causing complete loss of membrane potential after 10 min and of membrane integrity within 30 min, with irreversible damage to the cell as shown by rapid loss of viability. The number of particles, measured by light scatter on the flow cytometer, dropped significantly, showing that bacterial lysis resulted. The peptide was shown to bind to E. coli O111 lipopolysaccharide by using surface plasmon resonance. Transmission electron microscopy revealed bacterial distortion, with the outer membrane becoming detached from the inner cytoplasmic membrane. We conclude that HLP 2 causes membrane disruption of the outer membrane, resulting in lysis, and that structural considerations are important for antibacterial activity.
Citation: 2

Antibacterial activity of peptides homologous to a loop region in human lactoferrin

Cited Entries: LFH0045, LFH0054, LFH0079

Authors:Odell, E.W., Sarra, R., Foxworthy, M., Chapple, D.S., Evans, R.W.
Journal: FEBS Letters 1996, 382(1-2).
CrossRef External Link
Abstract: Human lactoferrin contains a 46 residue sequence named lactoferricin H thought to be responsible for its antimicrobial properties. Synthetic peptides HLT1, corresponding to the loop region of human lactoferricin (FQWQRNMRKVRGPPVS) and HLT2, corresponding to its charged portion (FQWQRNMRKVR), exerted significant antibacterial effects against E. coli serotype O111 strains NCTC 8007 and ML35. The corresponding sequences in native human lactoferrin were shown to adopt a charged helix and hydrophobic tall within the N-lobe remote from the iron binding site. Sequence similarities between lactoferricin and dermaseptin and magainins suggest that lactoferricin may act as an amphipathic alpha helix.
Keywords: Lactoferrin; Lactoferricin; Antimicrobial peptides
Citation: 3

Human lactoferrin and peptides derived from its N terminus are highly effective against infections with antibiotic-resistant bacteria

Cited Entries: LFH0004, LFH0045, LFH0097, LFH0098, LFH0099, LFH0100

Authors:Nibbering, P.H., Ravensbergen, E., Welling, M.M., van Berkel, L.A., van Berkel, P.H.C., Pauwels, E.K.J., Nuijens, J.H.
Journal: Infection and Immunity 2001, 69(3).
Abstract: Since human lactoferrin (hLF) binds to bacterial products through its highly positively charged N terminus, we investigated which of the two cationic domains is involved in its bactericidal activity. The results revealed that hLF lacking the first three residues (hLF[-]3N) was less efficient than hLF in killing of antibiotic-resistant Staphylococcus aureus, Listeria monocytogenes, and Klebsiella pneumoniae. Both hLF preparations failed to kill Escherichia coli O54. In addition, hLF[-]3N was less effective than hLF in reducing the number of viable bacteria in mice infected with antibiotic-resistant S. aureus and K. pneumoniae. Studies with synthetic peptides corresponding to the first 11 N-terminal amino acids, designated hLF(1-11), and fragments thereof demonstrated that peptides lacking the first three N-terminal residues are less effective than hLF(1-11) in killing of bacteria. Furthermore, a peptide corresponding to residues 21 to 31, which comprises the second cationic domain, was less effective than hLF(1-11) in killing of bacteria in vitro and in mice having an infection with antibiotic-resistant S. aureus or K. pneumoniae. Using fluorescent probes, we found that bactericidal hLF peptides, but not nonbactericidal peptides, caused an increase of the membrane permeability. In addition, hLF killed the various bacteria, most probably by inducing intracellular changes in these bacteria without affecting the membrane permeability. Together, hLF and peptides derived from its N terminus are highly effective against infections with antibiotic-resistant S. aureus and K. pneumoniae, and the first two arginines play an essential role in this activity.
Citation: 4

Structure and association of human lactoferrin peptides with Escherichia coli lipopolysaccharide

Cited Entries: LFH0045, LFH0048

Authors:Chapple, D.S., Hussain, R., Joannou, C.L., Hancock, R.E.W., Odell, E., Evans, R.W., Siligardi, G.
Journal: Antimicrobial Agents and Chemotherapy 2004, 48(6).
Abstract: An 11-amino-acid amphipathic synthetic peptide homologous to a helical region on helix 1 of human lactoferrin HLP-2 exhibited bactericidal activity against Escherichia coli serotype O111, whereas an analogue synthesized with Pro substituted for Met, HLP-6, had greatly reduced antimicrobial activity. The bactericidal activity of HLP-2 was 10-fold greater than that of HLP-6 in both buffer and growth medium by time-kill assays. These assays also showed a pronounced lag phase that was both concentration and time dependent and that was far greater for HLP-2 than for HLP-6. Both peptides, however, were shown to be equally efficient in destabilizing the outer membrane when the hydrophobic probe 1-N-phenylnaphthylamine was used and to have the same lipopolysaccharide (LPS) binding affinity, as shown by polymyxin B displacement. Circular dichroism (CD) spectroscopy was used to study the structure and the organization of the peptides in solution and upon interaction with E. coli LPS. In the presence of LPS, HLP-2 and HLP-6 were found to bind and adopt a {beta}-strand conformation rather than an {alpha}-helix, as shown by nonimmobilized ligand interaction assay-CD spectroscopy. Furthermore, this assay was used to show that there is a time-dependent association of peptide that results in an ordered formation of peptide aggregates. The rate of interpeptide association was far greater in HLP-2 LPS than in HLP-6 LPS, which was consistent with the lag phase observed on the killing curves. These results allow us to propose a mechanism by which HLP-2 folds and self-assembles at the outer membrane surface before exerting its activity.
Citation: 5

Variation in antimicrobial activity of lactoferricin-derived peptides explained by structure modelling

Cited Entries: LFH0045, LFB0109

Authors:Farnaud, S., Patel, A., Odell, E.W., Evans, R.W.
Journal: FEMS Microbiology Letters 2004, 238(1).
Abstract: Antimicrobial peptides bovine lactoferricin (LfcinB) and human lactoferricin (LfcinH) are produced from the respective lactoferrin, but are more active than their precursors. Despite sequence homology, the bovine peptide and its derivatives are more active than their human homologs. Such differences between not only the peptides and their precursor but also between the bovine and the human peptides could relate to structural differences. Upon sequence alignment of both peptides with their parental proteins, the structural differences observed between the bovine lactoferrin (BLf) and LfcinB were also found between the human lactoferrin (HLf) and the LfcinH. The helical structures in HLf are replaced by beta-strands separated by a strong turn in LfcinH suggesting an antiparallel beta-sheet structure similar to LfcinB. MIC assays with HLP-2 and BLP-2, 11-residue peptides derived from the active core of both Lfcins, against Escherichia coli, showed that the bovine derivative, BLP-2, is more active than its human homolog HLP-2. Both 3D models for HLP-2 and BLP-2 showed that the beta-strand is centred between the aromatic residues giving both side chains the same orientations. The displacement towards the N-terminus observed for the beta-strand in HLP-2, compared with its central location in BLP-2, could be less favourable to membrane interaction and therefore responsible for the decrease in activity. Such a model suggests for LfcinH a mechanism similar to the one observed for LfcinB, where the absence of long-range interaction, present in lactoferrin, destabilises the first alpha helix, as observed in solution and, upon interaction with the membrane, could result in the formation of a beta-strand, as observed in the presence of LPS. The location of the beta-strand in relation to the positive charges, seems to define the efficiency of the activity of the peptide and may explain the difference in activity obtained between HLP-2 and BLP-2.
Keywords: Lactoferrin; Lactoferricin; Cationic antimicrobial peptides; Lps; Modeller
Citation: 6

Structure-microbicidal activity relationship of synthetic fragments derived from the antibacterial alpha-helix of human lactoferrin

Cited Entries: LFH0011, LFH0012, LFH0013, LFH0014, LFH0015, LFH0021, LFH0027, LFH0029, LFH0030, LFH0031, LFH0032, LFH0033, LFH0034, LFH0035, LFH0036, LFH0037, LFH0038, LFH0039, LFH0040, LFH0041, LFH0045, LFH0055, LFH0066, LFH0067, LFH0068, LFH0069, LFH0070, LFH0071, LFH0072, LFH0073, LFH0074, LFH0075, LFH0076, LFH0077, LFH0078

Authors:Haversen, L., Kondori, N., Baltzer, L., Hanson, L.A., Dolphin, G.T., Duner, K., Mattsby-Baltzer, I.
Journal: Antimicrobial Agents and Chemotherapy. 2010, 54(1).
Abstract: There is a need for new microbicidal agents with therapeutic potential due to antibiotic resistance in bacteria and fungi. In this study, the structure-microbicidal activity relationship of amino acid residues 14 to 31 (sequence 14-31) from the N-terminal end, corresponding to the antibacterial {alpha}-helix of human lactoferrin (LF), was investigated by downsizing, alanine scanning, and substitution of amino acids. Microbicidal analysis (99% killing) was performed by a microplate assay using Escherichia coli, Staphylococcus aureus, and Candida albicans as test organisms. Starting from the N-terminal end, downsizing of peptide sequence 14-31 showed that the peptide sequence 19-31 (KCFQWQRNMRKVR, HL9) was the optimal length for antimicrobial activity. Furthermore, HL9 bound to lipid A/lipopolysaccharide, as shown by neutralizing endotoxic activity in a Limulus assay. Alanine scanning of peptide sequence 20-31 showed that Cys20, Trp23, Arg28, Lys29, or Arg31 was important for expressing full killing activity, particularly against C. albicans. Substituting the neutral hydrophilic amino acids Gln24 and Asn26 for Lys and Ala (HLopt2), respectively, enhanced microbicidal activity significantly against all test organisms compared to the amino acids natural counterpart, also, in comparison with HL9, HLopt2 had more than 10-fold-stronger fungicidal activity. Furthermore, HLopt2 was less affected by metallic salts than HL9. The microbicidal activity of HLopt2 was slightly reduced only at pH 7.0, as tested in the pH range of 4.5 to 7.5. The results showed that the microbicidal activity of synthetic peptide sequences, based on the antimicrobial {alpha}-helix region of LF, can be significantly enhanced by optimizing the length and substitution of neutral amino acids at specific positions, thus suggesting a sequence lead with therapeutic potential.
Citation: 7

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
Citation: 8

Enhancement of antibacterial and lipopolysaccharide binding activities of a human lactoferrin peptide fragment by the addition of acyl chain

Cited Entries: LFH0045, LFH0090, LFH0091, LFH0092, LFH0093, LFH0094, LFH0095, LFH0096

Authors:Majerle, A., Kidric, J., Jerala, R.
Journal: Journal of Antimicrobial Chemotherapy 2003, 51(5).
Abstract: Cationic antibacterial peptides are potentially therapeutic in the treatment of sepsis, because of their amalgamated antibacterial and lipopolysaccharide-binding activities. We prepared acyl analogues of the peptide fragment of human lactoferrin, which originally had weak antibacterial activity. It was found that 12 carbon units constitute the optimal acyl chain length, enhancing the antibacterial activity and binding of lipopolysaccharide by up to two orders of magnitude. Lactoferrin-based lipopeptides approached the activity of polymyxin B, a lipopeptide of natural origin, but were also active against Gram-positive bacteria.
Citation: 9

Antibacterial activity of multiple antigen peptides homologous to a loop region in human lactoferrin

Cited Entries: LFH0045, LFH0050, LFH0051, LFH0052, LFH0053

Authors:Azuma, M., Del Carpio, C.A., Kojima, T., Yokoyama, I., Tajiri, H., Yoshikawa, K., Saga, S.
Journal: The Journal of Peptide Research 1999, 54(3).
Keywords: Antibacterial activity; Lactoferrin; multiple antigen peptide; pore formation

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