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LF f(20-35) modified [id=LAG0009]

Synonym: LF f(20-35)-R5

Producer Organism : Native Protein : Production Method :
Goat Lactoferrin (LF) Enzymatic hydrolysis and Purification with LC method/Synthetic
Activity : No activity detected
Target Organisms :

NOTE: No activity against Escherichia coli O111 .

Description :
Production method: Pepsin hydrolysis and purification with LC method/Synthetic.

Deletion of the fifth residue.
The sequence of the antimicrobial peptide from Korean Native goat lactoferrin (LAG0008) showed 75% and 44% similarity with bLF f(20-35) and hLF f(21-36).
In an effort to identify the amino acid residues essential for the antimicrobial activity, five derivatives were synthesized and their MIC values were compared. LAG0009, LAG0010 and LAG0013 did not show any antimicrobial activity even at concentrations greater than 1.0 mg/ml. All of these peptides have an arginine residue deleted in the cluster of positively charged residues between the 24th and 28th amino acid residues. Therefore, it seems that the part with the sequence RRMRK (2428) is essential for the activity against the bacterial strain used in this experiment (Citation: 1).
Length : 15 Mass (Da): 1 835.81 Common Amino Acids : RQ
Isolectric Point : 11.53 Net Charge : 3 Absent Amino Acids : CDEFHNV
Basic Residues : 3 Acidic Residues : 0 Hydrophobic Residues : 4
Polar Residues : 4 Boman Index : -35.31 Hydropathy Index : -0.907
Aliphatic Index : 58.67 Instability Index : 0 Extinction Coefficient : 6990
Absorbance 280nm : 499.29

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 LAG0001 100.0%  PEWSKCYQWQRRMRKLGAPSITCVRRTSA 
 2 LAG0004 100.0%  ---SKCYQWQRRMRKLGAPSITCVRRTS- 
 3 LAG0011  93.8%  ------YQWQRRMR-LGAPSIT------- 
 4 LAG0012 100.0%  --------WQRRMRKLGAPSIT------- 
 5 LAG0013  92.9%  --------WQRRM-KLGAPSIT------- 
 6 LAG0010  93.8%  ------YQWQRRM-KLGAPSIT------- 
 7 LAG0008 100.0%  ------YQWQRRMRKLGAPSIT------- 
 8 LAG0009  93.8%  ------YQWQR-MRKLGAPSIT------- 
 9 LAG0005 100.0%  ---SKCYQWQRRMRKLGAPSITCVRRTS- 

10 LAG0006 100.0%  ---SKCYQWQRRMRKLGAPSITCVRRTS- 

11 LAG0002 100.0%  ---SKCYQWQRRMRKLGA----------- 
12 LAG0003  93.3%  ---SKCYQWQWRMRKLGA----------- 

13 LAG0007 100.0%  ------YQWQRRMRKL------------- 

Citation: 1

Antimicrobial peptide of Korean native goat lactoferrin and identification of the part essential for this activity

Cited Entries: LAG0008, LAG0009, LAG0010, LAG0011, LAG0012, LAG0013

Authors:Kimura, M., Nam, M.-S., Ohkouchi, Y., Kumura, H., Shimazaki, K.-I., Yu, D.-Y.
Journal: Biochemical and Biophysical Research Communications 2000, 268(2).
CrossRef External Link
Abstract: The antimicrobial activity of lactoferrin isolated from Korean native goat (KN goat) milk was studied and its antimicrobial domain was identified using synthetic peptides. Antimicrobial activity was assayed by a micro-method using 96-well microplates and a microplate reader. The amino acid sequence of the antimicrobial domain was suggested to be YQWQRRMRKLGAPSIT and this sequence corresponds to amino acid residues 20 to 35 of KN goat lactoferrin. Five peptides with certain amino acid residues deleted were synthesized in an effort to identify the residues essential for antimicrobial activity and it was found that the part with the sequence RRMRK (2428) is the region most important for this activity. On the other hand, the conformation of the peptides did not influence the antimicrobial activity.

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