LF f(31-35) [id=LFH0079]

Synonym: HLT5

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

NOTE: No activity against Escherichia coli 8007, Escherichia coli ML35(>500 ÁM) .

Description :
Production method: Synthetic.

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: 1).
Length : 5 Mass (Da): 455.54 Common Amino Acids : P
Isolectric Point : 6.11 Net Charge : Absent Amino Acids : ACDEFHIKLMNQRTWY
Basic Residues : 0 Acidic Residues : 0 Hydrophobic Residues : 1
Polar Residues : 2 Boman Index : 1.58 Hydropathy Index : -0.04
Aliphatic Index : 58 Instability Index : 0 Extinction Coefficient :
Absorbance 280nm : 0

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

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

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