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LF f(17-30) [id=LFB0030]

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

Gram-positive: Active against Staphylococcus aureus ATCC 25923, Staphylococcus aureus MRSA at 20 然, Staphylococcus aureus HG386 (MIC=75 痢/ml), Streptococcus mutans HG455 (MIC=37 痢/ml), Streptococcus mutans Ingbritt (LC50=5.5 然), Streptococcus sobrinus OB50 (MIC=37 痢/ml), Streptococcus salivarius HG475 (MIC=37 痢/ml), Streptococcus sanguis SK4 (LC50=5.5 然), Bacillus subtilis ATCC 9372 (LC50=10 然), Actinomyces naeslundii ATCC 12104 (LC50=10 然).

Gram-negative: Active against Escherichia coli EPEC E2348/69, Escherichia coli MREPEC, Escherichia coli EHEC O157:H7 at 20 然, Escherichia coli K12 (MIC=37 痢/ml or LC50=1.8 然), Escherichia coli O157:H7 (LC50=1.9 然), Klebsiella pneumoniae HG389 (MIC=75 痢/ml), Prevotella intermedia OB51 (MIC=18 痢/ml), Porphyromonas gingivalis W83 (MIC=1250 痢/ml or MIC>100 然), Fusobacterium nucleatum (HG410) (MIC=1250 痢/ml), Pseudomonas aeruginosa PAO (LC50=2.9 然), Pseudomonas aeruginosa PAK (LC50=1.5 然).

Yeast: Candida albicans 315 ATCC 10231 (LC50=1.5 然), Candida albicans A2 (MIC=10 然), Candida albicans A6 (MIC=5 然).

Parasite: Active against Entamoeba histolytica (no value), Leishmania donovani (IC50=21.9 然 or LC50=25.3 然).

NOTE: No activity against Aggregatibacter actinomycetemcomitans OB43 (>5 mg/ml on agar plate), Helicobacter pylori (>1.2 然), Leishmania pifanoii (>50 然) .

Description :
Production method: Synthetic.
See LFB0031.
Length : 14 Mass (Da): 1 923.75 Common Amino Acids : KR
Isolectric Point : 12.26 Net Charge : 6 Absent Amino Acids : ADEHINPSTVY
Basic Residues : 6 Acidic Residues : 0 Hydrophobic Residues : 4
Polar Residues : 2 Boman Index : -49.82 Hydropathy Index : -1.421
Aliphatic Index : 27.86 Instability Index : 0 Extinction Coefficient : 11000
Absorbance 280nm : 846.15

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 [        .         .         . ] 32
  1 LFBNATIVE 100.0%    FKCRRWQWRMKKLGAPSITCVRRAFALECIRA   
  2 LFB0017   100.0%    FKCRRWQWR-----------------------   
  3 LFB0043    93.3%    FKCRRWQWRAKKLGA-----------------   
  4 LFB0052    86.7%    FKCWRWQWRWKKLGA-----------------   
  5 LFB0037    93.3%    FKCARWQWRMKKLGA-----------------   
  6 LFB0040    93.3%    FKCRRWAWRMKKLGA-----------------   
  7 LFB0038    93.3%    FKCRAWQWRMKKLGA-----------------   
  8 LFB0088    96.0%    FKCRRWQWRMKKLGAPSITCVRRAE-------   
  9 LFB0039    93.3%    FKCRRAQWRMKKLGA-----------------   
 10 LFB0062    93.3%    FKCRRAQWRMKKLGA-----------------   
 11 LFB0072    93.3%    FKCRRAQWRMKKLGA-----------------   
 12 LFB0075    93.3%    FKCRRAQWRMKKLGA-----------------   
 13 LFB0078    93.3%    FKCRRAQWRMKKLGA-----------------   
 14 LFB0064    86.7%    FKCRRAQARMKKLGA-----------------   
 15 LFB0117    54.5%    ---RRAAARAKKAG------------------   
 16 LFB0080    86.7%    FKCRRAQARMKKLGA-----------------   
 17 LFB0074    86.7%    FKCRRAQARMKKLGA-----------------   
 18 LFB0077    86.7%    FKCRRAQARMKKLGA-----------------   
 19 LFB0056    93.3%    FKCRRFQWRMKKLGA-----------------   
 20 LFB0059    93.3%    FKCRRFQWRMKKLGA-----------------   
 21 LFB0053    93.3%    FKCRRFQWRMKKLGA-----------------   
 22 LFB0081    93.3%    FKCRRFQWRMKKLGA-----------------   
 23 LFB0055    86.7%    FKCRRFQFRMKKLGA-----------------   
 24 LFB0058    86.7%    FKCRRFQFRMKKLGA-----------------   
 25 LFB0061    86.7%    FKCRRFQFRMKKLGA-----------------   
 26 LFB0083    86.7%    FKCRRFQFRMKKLGA-----------------   
 27 LFB0041    93.3%    FKCRRWQARMKKLGA-----------------   
 28 LFB0063    93.3%    FKCRRWQARMKKLGA-----------------   
 29 LFB0076    93.3%    FKCRRWQARMKKLGA-----------------   
 30 LFB0079    93.3%    FKCRRWQARMKKLGA-----------------   
 31 LFB0073    93.3%    FKCRRWQARMKKLGA-----------------   
 32 LFB0060    93.3%    FKCRRWQFRMKKLGA-----------------   
 33 LFB0082    93.3%    FKCRRWQFRMKKLGA-----------------   
 34 LFB0057    93.3%    FKCRRWQFRMKKLGA-----------------   
 35 LFB0054    93.3%    FKCRRWQFRMKKLGA-----------------   
 36 LFB0042    93.3%    FKCRRWQWAMKKLGA-----------------   
 37 LFB0115    81.8%    ---RRWQRWMKKLG------------------   
 38 LFB0033   100.0%    FKCRRWQWRMKKLGA-----------------   
 39 LFB0032   100.0%    FKCRRWQWRMKKLGA-----------------   
 40 LFB0031   100.0%    FKCRRWQWRMKKLGA-----------------   
 41 LFB0050    86.7%    FKWRRWQWRMKKLWA-----------------   
 42 LFB0051    80.0%    FKWRRWWWRMKKLWA-----------------   
 43 LFB0049    93.3%    FKCRRWQWRMKKLWA-----------------   
 44 LFB0018   100.0%    FKCRRWQWRM----------------------   
 45 LFB0020   100.0%    FKCRRWQWRMK---------------------   
 46 LFB0045    93.3%    FKCRRWQWRMKALGA-----------------   
 47 LFB0044    93.3%    FKCRRWQWRMAKLGA-----------------   
 48 LFB0097   100.0%    ---RRWQWR-----------------------   
 49 LFB0030   100.0%    FKCRRWQWRMKKLG------------------   
 50 LFB0087   100.0%    FKCRRWQWRMKKLGAPSITCVRRAF-------   
 51 LFB0024    54.5%    YKAWRWAWRWK---------------------   
 52 LFB0025    54.5%    YKAWRWAWRWK---------------------   
 53 LFB0027    36.4%    YRMWRWAWRWR---------------------   
 54 LFB0028    36.4%    YRMWRWRWRWR---------------------   
 55 LFB0026    36.4%    YRAWRWAWRWR---------------------   
 56 LFB0023    63.6%    YKARRWAWRWK---------------------   
 57 LFB0022    72.7%    YKARRWAWRMK---------------------   
 58 LFB0021    81.8%    FKARRWAWRMK---------------------   
 59 LFB0019    90.0%    FKARRWQWRM----------------------   
 60 LFB0036    93.3%    FKARRWQWRMKKLGA-----------------   
 61 LFB0070    93.3%    FKARRWQWRMKKLGA-----------------   
 62 LFB0069    93.3%    FKARRWQWRMKKLGA-----------------   
 63 LFB0068    93.3%    FKARRWQWRMKKLGA-----------------   
 64 LFB0065    93.3%    FKARRWQWRMKKLGA-----------------   
 65 LFB0106   100.0%    ---RRWQWRMKK--------------------   
 66 LFB0029    45.5%    RRWYRWAWRMR---------------------   
 67 LFB0118   100.0%    ----RWQWRM----------------------   
 68 LFB0113    81.8%    ---RRWQWRMRRLG------------------   
 69 LFB0112    72.7%    ---KKWQWKMKKLG------------------   
 70 LFB0114    81.8%    ---KKWQWRMKKLG------------------   
 71 LFB0116    54.5%    ---EEWQWEMEELG------------------   
 72 LFB0048    93.3%    FKWRRWQWRMKKLGA-----------------   
 73 LFB0090    92.0%    FKSRRWQWRMKKLGAPSITSVRRAF-------   
 74 LFB0110    18.2%    ----RRWQWRMKKLG-----------------   
 75 LFB0067    93.3%    FKFRRWQWRMKKLGA-----------------   
 76 LFB0071    93.3%    FKFRRWQWRMKKLGA-----------------   
 77 LFB0066    93.3%    FKFRRWQWRMKKLGA-----------------   
 78 LFB0108   100.0%    ---RRWQWRMKKL-------------------   
 79 LFB0102   100.0%    ---RRWQWRMKK--------------------   
 80 LFB0034    93.3%    AKCRRWQWRMKKLGA-----------------   
 81 LFB0111   100.0%    ---RRWQWRMKKLG------------------   
 82 LFB0104   100.0%    ---RRWQWRMKK--------------------   
 83 LFB0035    93.3%    FACRRWQWRMKKLGA-----------------   
 84 LFB0109   100.0%    ---RRWQWRMKKLG------------------   
 85 LFB0101   100.0%    ---RRWQWRMKK--------------------   
 86 LFB0046    93.3%    FKCRRWQWRMKKAGA-----------------   
 87 LFB0107   100.0%    ---RRWQWRMKK--------------------   
 88 LFB0100   100.0%    ---RRWQWRMKK--------------------   
 89 LFB0047    93.3%    FKCRRWQWRMKKLAA-----------------   
 90 LFB0098   100.0%    ---RRWQWRMKK--------------------   
 91 LFB0105   100.0%    ---RRWQWRMKK--------------------   
 92 LFB0103   100.0%    ---RRWQWRMKK--------------------   
 93 LFB0086   100.0%    FKCRRWQWRMKKLGAPSITCVRRAF-------   
 94 LFB0089   100.0%    FKCRRWQWRMKKLGAPSITCVRRAF-------   
 95 LFB0085   100.0%    FKCRRWQWRMKKLGAPSITCVRRAF-------   
 96 LFB0084   100.0%    FKCRRWQWRMKKLGAPSITCVRRAF-------   
 97 LFB0092   100.0%    FKCRRWQWRMKKLGAPSITCVRRAFA------   
 98 LFB0095   100.0%    -KCRRWQWRMKKLGAPSITCV-----------   
 99 LFB0096   100.0%    --CRRWQWRMKKLGAPSITCV-----------   

100 LFB0093   100.0%    FKCRRWQWRMKKLGAPSITCVRRAFAL-----   

101 LFB0091   100.0%    FKCRRWQWRMKKLGAPSITCVRRAFA------   

102 LFB0119   100.0%    ----------KKLGAPSITCVRRAFA------   
103 LFB0120   100.0%    -------------GAPSITCVRRAF-------   

104 LFB0121   100.0%    ----------------------------CIRA   
105 LFB0094   100.0%    FKCRRWQWRMKKLGAPSITCVRRAFALECIR-   

Citation: 1

Lactoferrampin: a novel antimicrobial peptide in the N1-domain of bovine lactoferrin

Cited Entries: LFB0030, LFB0149, LFB0157, LFB0158

Authors:van der Kraan, M.I.A., Groenink, J., Nazmi, K., Veerman, E.C.I., Bolscher, J.G.M., Nieuw Amerongen, A.V.
Journal: Peptides 2004, 25(2).
CrossRef External Link
Abstract: The antimicrobial activity of bovine lactoferrin is attributed to lactoferricin, situated in the N1-domain. Based on common features of antimicrobial peptides, a second putative antimicrobial domain was identified in the N1-domain of lactoferrin, designated lactoferrampin. This novel peptide exhibited candidacidal activity, which was substantially higher than the activity of lactoferrin. Furthermore, lactoferrampin was active against Bacillus subtilis, Escherichia coli, and Pseudomonas aeruginosa, but not against the fermenting bacteria Actinomyces naeslundii, Porphyromonas gingivalis, Streptococcus mutans and Streptococcus sanguis. Notably, lactoferrampin is located in the N1-domain in close proximity to lactoferricin, which plays a crucial role in membrane-mediated activities of lactoferrin.
Keywords: antimicrobial peptide; Lactoferrin; Lactoferricin; Lactoferrampin; C.albicans; Gram-positive bacteria; Gram-negative bacteria
Citation: 2

Cationic amphipathic peptides, derived from bovine and human lactoferrins, with antimicrobial activity against oral pathogens

Cited Entries: LFH0021, LFH0042, LFB0030, LFB0096

Authors:Groenink, J., Walgreen-Weterings, E., van 't Hof, W., Veerman, E.C., Nieuw Amerongen, A.V.
Journal: FEMS Microbiology Letters 1999, 179(2).
Abstract: Peptides derived from the N-terminal domain that comprises an amphipathic alpha-helix in human lactoferrin (LFh 18-31 and LFh 20-38) and bovine lactoferrin (LFb 17-30 and LFb 19-37) were chemically synthesised. Since many positively charged amphipathic alpha-helices contain antimicrobial activity, the peptides were tested for their antimicrobial activity against various oral pathogens. Both peptides from bovine lactoferrin had more potent antimicrobial activities than the human equivalents. Peptide LFb 17-30, containing the largest number of positively charged amino acids, showed the highest antimicrobial activity to both Gram-positive and Gram-negative bacteria. Since native lactoferrin molecules had no killing activity, release of these peptides from the native protein should be investigated to explore the use in oral care products.
Keywords: Lactoferrin; antimicrobial peptide; Oral bacterium
Citation: 3

Bactericidal activity of LFchimera is stronger and less sensitive to ionic strength than its constituent lactoferricin and lactoferrampin peptides

Cited Entries: LFB0030, LFB0131, LFB0154

Authors:Bolscher, J.G.M., Adao, R., Nazmi, K., van den Keybus, P.A.M., van 't Hof, W., Nieuw Amerongen, A.V., Bastos, M., Veerman, E.C.I.
Journal: Biochimie 2009, 91(1).
CrossRef External Link
Abstract: The innate immunity factor lactoferrin harbours two antimicrobial moieties, lactoferricin and lactoferrampin, situated in close proximity in the N1 domain of the molecule. Most likely they cooperate in many of the beneficial activities of lactoferrin. To investigate whether chimerization of both peptides forms a functional unit we designed a chimerical structure containing lactoferricin amino acids 1730 and lactoferrampin amino acids 265284. The bactericidal activity of this LFchimera was found to be drastically stronger than that of the constituent peptides, as was demonstrated by the need for lower dose, shorter incubation time and less ionic strength dependency. Likewise, strongly enhanced interaction with negatively charged model membranes was found for the LFchimera relative to the constituent peptides. Thus, chimerization of the two antimicrobial peptides resembling their structural orientation in the native molecule strikingly improves their biological activity.
Keywords: antimicrobial peptide; bovine lactoferrin; Lactoferricin; Lactoferrampin; LFchimera; Dsc; Cd
Citation: 4

Lactoferrin-derived peptides and Lactoferricin chimera inhibit virulence factor production and biofilm formation in Pseudomonas aeruginosa

Cited Entries: LFB0030, LFB0149, LFB0155

Authors:Xu, G., Xiong, W., Hu, Q., Zuo, P., Shao, B., Lan, F., Lu, X., Xu, Y., Xiong, S.
Journal: Journal of Applied Microbiology 2010, 109(4).
Abstract: AIMS: To investigate the bactericidal activity of lactoferrin-derived peptides and a new LF-derived peptides chimera (LFchimera) against P. aeruginosa and the influence on virulence factors of P. aeruginosa. METHODS AND RESULTS: Lactoferricin (LFcin) and lactoferrampin (LFampin) are highly bioactive peptides isolated from the N-terminal region of lactoferrin (LF) by pepsin digestion. In this study, we designed LFchimera containing LFcin amino acids 17-30 and LFampin amino acids 268-284. Pseudomonas aeruginosa cells were incubated in medium with peptides at different concentrations, and then the assays of viability, pyocyanin, elastase activity and biofilm formation of P. aeruginosa were performed. We found that the concentration-dependent antibactericidal activity and down-regulating pyocyanin, elastase and biofilm formation of LFchimera were significantly stronger than those of LF, LFcin, LFampin or LFcin plus LFampin. CONCLUSIONS: Our results indicated that LF, LFcin, LFampin and LFchimera were potential candidates to combat P. aeruginosa, and LFchimera was the most effective in them. SIGNIFICANCE AND IMPACT OF THE STUDY: The new LFchimera has better activity against P. aeruginosa than LF, LFcin and LFampin and may be a promising new compound for treatment of P. aeruginosa infection.
Keywords: biofilm formation; Lactoferricin; lactoferricin chimera; Pseudomonas aeruginosa; virulence factor
Citation: 5

Fungicidal effect of three new synthetic cationic peptides against Candida albicans

Cited Entries: LFB0030

Authors:Nikawa, H., Fukushima, H., Makihira, S., Hamada, T., Samaranayake, L. P.
Journal: Oral Diseases 2004, 10(4): 8.
Abstract: Dhvar 4, showed the most a-helical propensity, and was the least fungicidal while LFB and LFB(1730) showed the highest antifungal potential, and demonstrated total kill of A6, and A2 at 5 and 10 lM concentrations, respectively whilst LFH killed both isolates at a l0 lM concentration. Of the three new synthetic peptides, JH 8194 was the most potent (total kill of A6/A2 strains at 1.25/2.5 lM), followed by JH 8195 (total kill of A6/A2 strains at 5/10 lM while JH 8944 was the least potent as a 25 lM concentration was required to kill either strain of Candida. On further analyses of the relationship between pI value of the peptides and their anticandicidal activity, a significant positive correlation was noted. In order to rule out a cytotoxic effect of the new synthetic peptides we compared the fungicidal and hemolytic activities under similar incubation conditions using freshly isolated erythrocytes and all three peptides exhibited no detectable hemolysis upto an concentration of 100 lM in contrast to the polyene antifungal amphotericin B that elicited significant initiation of hemolysis at a concentration of 5.0 lM.
Keywords: cationic peptide; antifungal activity; Candida albicans
Citation: 6

Bactericidal effect of bovine lactoferrin, LFcin, LFampin and LFchimera on antibiotic-resistant Staphylococcus aureus and Escherichia coli

Cited Entries: LFB0030, LFB0131, LFB0154

Authors:Flores-Villasenor, H., Canizalez-Roman, A., Reyes-Lopez, M., Nazmi, K., de la Garza, M., Zazueta-Beltran, J., Leon-Sicairos, N., Bolscher, J.G.
Journal: BioMetals 2010, 23(3).
Abstract: Increased prevalence of antibiotic-resistant bacteria has become a major threat to the health sector worldwide due to their virulence, limited therapeutic options and distribution in both hospital and community settings. Discovery and development of new agents to combat antibiotic-resistant bacteria is thus needed. This study therefore aimed to evaluate the ability of bovine lactoferrin (LF), peptides from two antimicrobial domains lactoferricin B (LFcin17-30) and lactoferrampin (LFampin265-284) and a chimeric construct (LFchimera) containing both peptides, as potential bactericidal agents against clinical isolates of antibiotic-resistant Staphylococcus aureus and Escherichia coli. Results in kinetics of growth show that LF chimera and peptides inhibited the growth of both bacterial species. By confocal microscopy and flow cytometry it was observed that LF and FITC-labeled peptides are able to interact with these bacteria and cause membrane permeabilization, as monitored by propidium iodide staining, these effects were decreased by preincubation with lipopolysaccharide in E. coli. By electron microscopy, a clear cellular damage was observed in bacteria after treatments with LFchimera and peptides, suggesting that interaction and membrane disruption are probably involved as a mechanism of action. In conclusion, results show that LFchimera, LF and peptides have potential as bactericidal agents in the antibiotic-resistant strains of S. aureus and E. coli and also the work strongly suggest that LFcin17-30 and LFampin265-284 acts synergistically with antibiotics against multidrug resistant EPEC and MRSA in vitro.
Keywords: Chemistry and Materials Science
Citation: 7

Chimerization of lactoferricin and lactoferrampin peptides strongly potentiates the killing activity against Candida albicans

Cited Entries: LFB0030, LFB0131, LFB0154

Authors:Bolscher, J., Nazmi, K., van Marle, J., van t Hof, W., Veerman, E.
Journal: Biochemistry and Cell Biology 2012, 90(3): 11.
Abstract: Bovine lactoferrin harbors 2 antimicrobial sequences (LFcin and LFampin), situated in close proximity in the N1- domain. To mimic their semi parallel configuration we have synthesized a chimeric peptide (LFchimera) in which these sequences are linked in a head-to-head fashion to the a- and 3-amino group, respectively, of a single lysine. In line with previously described bactericidal effects, this peptide was also a stronger candidacidal agent than the antimicrobial peptides LFcin1730 and LFampin265284, or a combination of these 2. Conditions that strongly reduced the candidacidal activities of LFcin1730 and LFampin265284, such as high ionic strength and energy depletion, had little influence on the activity of LFchimera. Freeze-fracture electron microscopy showed that LFchimera severely affected the membrane morphology, resulting in disintegration of the membrane bilayer and in an efflux of small and high molecular weight molecules such as ATP and proteins. The differential effects displayed by the chimeric peptide and a mixture of its constituent peptides clearly demonstrate the synergistic effect of linking these peptides in a fashion that allows a similar spatial arrangement as in the parent protein, suggesting that in bovine lactoferrrin the corresponding fragments act in concert in its candidacidal activity
Keywords: Candida albicans, yeast, pseudohyphae, lactoferricin, lactoferrampin, LFchimera
Citation: 8

Enhanced leishmanicidal activity of cryptopeptide chimeras from the active N1 domain of bovine lactoferrin

Cited Entries: LFB0030, LFB0131, LFB0154, LFB0173, LFB0174, LFB0175, LFB0176, LFB0177

Authors:Silva, T., Abengozar, M. A., Fernandez-Reyes, M., Andreu, D., Nazmi, K., Bolscher, J. G. M., Bastos, M., Rivas, L.
Journal: Amino acids 2012,.
Abstract: Two antimicrobial cryptopeptides from the N1 domain of bovine lactoferrin, lactoferricin (LFcin1730) and lactoferrampin (LFampin265284), together with a hybrid version (LFchimera), were tested against the protozoan parasite Leishmania. All peptides were leishmanicidal against Leishmania donovani promastigotes, and LFchimera showed a significantly higher activity over its two composing moieties. Besides, it was the only peptide active on Leishmania pifanoi axenic amastigotes, already showing activity below 10 lM. To investigate their leishmanicidal mechanism, promastigote membrane permeabilization was assessed by decrease of free ATP levels in living parasites, entrance of the vital dye SYTOX Green (MW = 600 Da) and confocal and transmission electron microscopy. The peptides induced plasma membrane permeabilization and bioenergetic collapse of the parasites. To further clarify the structural traits underlying the increased leishmanicidal activity of LFchimera, the activity of several analogues was assessed. Results revealed that the high activity of these hybrid peptides seems to be related to the order and sequence orientation of the two cryptopeptide moieties, rather than to their particular linkage through an additional lysine, as in the initial LFchimera. The incorporation of both antimicrobial cryptopeptide motifs into a single linear sequence facilitates chemical synthesis and should help in the potential clinical application of these optimized analogues.
Keywords: Leishmania; Leishmanicidal activity; Antimicrobial peptides; Membrane permeabilization; Lactoferricin; Lactoferrampin; LFchimera
Citation: 9

Bactericidal effect of lactoferrin and lactoferrin chimera against halophilic Vibrio parahaemolyticus

Cited Entries: LFB0030, LFB0131, LFB0154

Authors:Leon-Sicairosa, N., Canizalez-Romanb, A., de la Garzac, M., Reyes-Lopez, M., Zazueta-Beltrand, J., Nazmif, K., Gomez-Gile, B., Bolscher, J. G.
Journal: Biochimie 2009, 91(1): 8.
Abstract: Infections caused by Vibrio parahaemolyticus, an halophilic member of the genus Vibrio, have increased globally in the last 5 years. Diarrhea caused by V. parahaemolyticus results from eating raw or undercooked seafood. The aim of this work was to investigate whether lactoferrin and some lactoferrin-peptides have bactericidal activity against Vibrio parahaemolyticus ATCC 17802, the pandemic strain O3:K6, and the multidrug resistant isolate 727, as well as against Vibrio cholerae strains O1 and non-O1. Whereas both peptides lactoferricin (1730) and lactoferrampin (265284) did not have bactericidal activity, 40 μM of lactoferrin chimera (a fusion of the two peptides) inhibited the growth of all Vibrio tested to the same extent as the antibiotic gentamicin. The cidal effect of LFchimera showed a clear concentration response in contrast to bovine lactoferrin which showed higher inhibition at 10 μM than at 40 μM. FITC-labeled LFchimera bound to the bacterial membranes. Moreover LFchimera permeabilized bacterial cells and membranes were seriously damaged. Finally, in experiments with the multidrug resistant isolate 727, sub-lethal doses of LFchimera strongly reduced the concentrations of ampicillin, gentamicin or kanamicin needed to reach more than 95% growth inhibition, suggesting synergistic effects. These data indicate that LFchimera is a potential candidate to combat the multidrug resistant pathogenic Vibrio species.
Keywords: Lactoferrin; Lactoferricin; Lactoferrampin; LFchimera; Vibrio parahaemolyticus
Citation: 10

Microbicidal effect of the lactoferrin peptides Lactoferricin1730, Lactoferrampin265284, and Lactoferrin chimera on the parasite Entamoeba histolytica

Cited Entries: LFB0030, LFB0131, LFB0154

Authors:Lopez-Soto, F., Leon-Sicairos, N., Nazmi, K., Bolscher, J. G., de la Garza, M.
Journal: Biometals 2010, 23: 6.
Abstract: Entamoeba histolytica is a parasitic protozoan that produces amoebiasis, an intestinal disease characterized by ulcerative colitis and dysentery. In some cases, trophozoites can travel to the liver leading to hepatic abscesses and death. Recently, lactoferrin and lactoferricin B have been shown to be amoebicidal in axenic cultures. The aim of this work was to determine whether the lactoferrin-peptides lactoferricin amino acids 1730, lactoferrampin amino acids 265284, and lactoferrin chimera which is a fusion product of the two peptides, are capable of producing a microbicidal effect to trophozoites of E. histolytica. We evaluated the killing effect of these peptides in growth kinetics carried out in axenic culture medium to which different concentrations of peptides were added. At 50 lM of peptide concentration, lactoferricin and lactoferrampin had a moderate amoebicidal effect, since a 4550% of trophozoites remained viable at 24 h culture. However, at 50 lM of the lactoferrin chimera 75% amoeba were killed whereas at 100 lM all cells died. These data indicate that of lactoferrin-peptides mainly the chimera have amoebicidal activity in a time- and concentration-dependent manner. The lactoferrin-peptides might be useful as therapeutic agents against amoebiasis and thereby diminish the use of metronidazole, which is extremely toxic for the host.
Keywords: Entamoeba histolytica; Amoebicidal effect, LFcin; LFampin; LFchimera

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