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LF f(5-11) [id=LFH0100]

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

NOTE: No activity against Staphylococcus aureus 2141, Listeria monocytogenes EGD, Klebsiella pneumoniae ATCC 43816, Escherichia coli O54 (>50 ÁM) .

Length : 7 Mass (Da): 849.28 Common Amino Acids : ASRVWQC
Isolectric Point : 8.55 Net Charge : 1 Absent Amino Acids : DEFGHIKLMNPTY
Basic Residues : 1 Acidic Residues : 0 Hydrophobic Residues : 3
Polar Residues : 2 Boman Index : -14.4 Hydropathy Index : -0.171
Aliphatic Index : 55.71 Instability Index : 0 Extinction Coefficient : 5500
Absorbance 280nm : 916.67

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.

Citation: 1

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.

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