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LF f(266-285) [id=LFH0063]

Synonym: Cap-LFampinH

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

NOTE: No activity against Candida albicans 315 ATCC 10231, Streptococcus sanguis SK4, Escherichia coli K12 (>50 M) .

Description :
Production method: Synthetic.

The human lactoferrampin amino acid sequence (LFH0061) that directly corresponds to the previously characterized bovine lactoferrin-derived lactoferrampin peptide (LFB0149) is inactive on its own. However, by increasing the net positive charge near the C-terminal end of human lactoferrampin, a significant increase in its antibacterial and Candidacidal activity was obtained (LFH0062). Conversely, the addition of an N-terminal helix cap (sequence DAI) did not have any appreciable effect on the antibacterial or antifungal activity of human lactoferrampin peptides (LFH0063, LFH0064), even though it markedly influenced that of bovine lactoferrampin (LFB0131, LFB0149). Finally, the cap-LFampH-K D17N peptide, with the negatively charged Asp in the C-terminus mutated to a neutral Asn residue, was more active against all three organisms tested compared to all of the other human variants (LFH0065) (Citation: 1).
Length : 20 Mass (Da): 2 345.30 Common Amino Acids : K
Isolectric Point : 9.44 Net Charge : 1 Absent Amino Acids : CHMTVY
Basic Residues : 4 Acidic Residues : 3 Hydrophobic Residues : 7
Polar Residues : 3 Boman Index : -52.31 Hydropathy Index : -1.12
Aliphatic Index : 68.5 Instability Index : 0 Extinction Coefficient : 5500
Absorbance 280nm : 289.47

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)

Identities computed with respect to: (1) LFH0064
Colored by: identity + property

1 LFH0064 100.0%  DAIWNLLRQAQEKFGKDKSPK 

2 LFH0061 100.0%  ---WNLLRQAQEKFGKDKSP- 

3 LFH0062 100.0%  ---WNLLRQAQEKFGKDKSPK 

4 LFH0063 100.0%  DAIWNLLRQAQEKFGKDKSP- 

5 LFH0065  95.2%  DAIWNLLRQAQEKFGKNKSPK 

Citation: 1

Novel lactoferrampin antimicrobial peptides derived from human lactoferrin

Cited Entries: LFH0061, LFH0062, LFH0063, LFH0064, LFH0065, LFB0131, LFB0149

Authors:Haney, E.F., Nazmi, K., Lau, F., Bolscher, J.G.M., Vogel, H.J.
Journal: Biochimie 2009, 91(1).
CrossRef External Link
Abstract: Human lactoferrampin is a novel antimicrobial peptide found in the cationic N-terminal lobe of the iron-binding human lactoferrin protein. The amino acid sequence that directly corresponds to the previously characterized bovine lactoferrin-derived lactoferrampin peptide is inactive on its own (WNLLRQAQEKFGKDKSP, residues 269285). However, by increasing the net positive charge near the C-terminal end of human lactoferrampin, a significant increase in its antibacterial and Candidacidal activity was obtained. Conversely, the addition of an N-terminal helix cap (sequence DAI) did not have any appreciable effect on the antibacterial or antifungal activity of human lactoferrampin peptides, even though it markedly influenced that of bovine lactoferrampin. The solution structure of five human lactoferrampin variants was determined in SDS micelles and all of the structures display a well-defined amphipathic N-terminal helix and a flexible cationic C-terminus. Differential scanning calorimetry studies indicate that this peptide is capable of inserting into the hydrophobic core of a membrane, while fluorescence spectroscopy results suggest that a hydrophobic patch encompassing the single Trp and Phe residues as well as Leu, Ile and Ala side chains mediates the interaction between the peptide and the hydrophobic core of a phospholipid bilayer.
Keywords: antimicrobial peptide; Human lactoferrin; Lactoferrampin; NUCLEAR magnetic resonance; Micelle-bound peptide structure

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