LF f(19-31) modified [id=LFH0082]

Synonym: LF f(19-31)6s

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

Gram-negative: Escherichia coli K12 D21e19 (MIC=320 然), Escherichia coli K12 D21e7 (MIC=320 然), Escherichia coli K12 W3110 (MIC=640 然), Escherichia coli K12 D21 (MIC=640 然), Escherichia coli K12 D21f1 (MIC=640 然), Escherichia coli K12 D21f2 (MIC=640 然), Escherichia coli MLK53 (MIC=640 然), Escherichia coli MLK1067 (MIC=320 然), Escherichia coli MLK986 (MIC=320 然), Escherichia coli WA707 (MIC=640 然), Escherichia coli WA834 (MIC=320 然).

Description :
Antimicrobial activity was obtained for two peptides LFH0081 and LFH0082 which were based on region 25-31 of human lactoferricin. They both contain five substitutions chosen from the bovine lactoferricin sequence.
Synthetic peptides derived from human and bovine lactoferricin, as well as tritrpticin sequences, were assayed for antimicrobial activity against wild-type Escherichia coli and LPS mutant strains. Antimicrobial activity was only obtained with peptides derived from the bovine lactoferricin sequence (LFH0016, LFH0017, LFH0018, LFH0019 and LFH0020) and peptides corresponding to chimeras of human (LFH0081 and LFH0082) and bovine sequences (LFB0031, LFB0041 and LFB0046). None of the peptides corresponding to different regions of native human lactoferricin showed any antimicrobial activity. The results underline the importance of the content of tryptophan and arginine residues, and the relative location of these residues for antimicrobial activity (Citation: 1).
Length : 13 Mass (Da): 1 752.26 Common Amino Acids : R
Isolectric Point : 12.98 Net Charge : 5 Absent Amino Acids : CDEFGHINQSTY
Basic Residues : 5 Acidic Residues : 0 Hydrophobic Residues : 5
Polar Residues : 0 Boman Index : -47.45 Hydropathy Index : -1.169
Aliphatic Index : 60 Instability Index : 0 Extinction Coefficient : 11000
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

Interactions of lactoferricin-derived peptides with LPS and antimicrobial activity

Cited Entries: LFH0002, LFH0003, LFH0016, LFH0017, LFH0018, LFH0019, LFH0020, LFH0056, LFH0080, LFH0081, LFH0082, LFH0083, LFH0084, LFB0031, LFB0041, LFB0046, LFB0097

Authors:Farnaud, S., Spiller, C., Moriarty, L.C., Patel, A., Gant, V., Odell, E.W., Evans, R.W.
Journal: FEMS Microbiology Letters 2004, 233(2).
Keywords: Lactoferrin; Lactoferricin; Cationic antimicrobial peptides; Lps; Mbc

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