General Information

    • DRAMP ID

    • DRAMP03635

    • Peptide Name

    • Human lactoferricin (LfcinH; one chain of Lactotransferrin; Human, mammals, animals)

    • Source

    • Homo sapiens (Human)

    • Family

    • Belongs to the transferrin family

    • Gene

    • LTF

    • Sequence

    • GRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQA

    • Sequence Length

    • 48

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram-

    • Target Organism

      • Gram-negative bacterium: Escherichia coli serotype O111.

    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Not included yet

    • N-terminal Modification

    • Not included yet

    • C-terminal Modification

    • Not included yet

    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet

    • Stereochemistry

    • Not included yet

    • Structure

    • Alpha helix

    • Structure Description

    • LfcinH shows a helical content from Gln14 to Lys29 in the membrane mimetic solvent but a nonexistent beta-sheet character in either the N- or C-terminal regions of the peptide. The LfcinH structure determined in aqueous solution displays a nascent helix in the form of a coiled conformation in the region from Gln14 to Lys29.

    • Helical Wheel Diagram

    • DRAMP03635 helical wheel diagram
  • 1Z6V-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP03635.

Physicochemical Information

    • Formula

    • C238H391N81O65S5

    • Absent Amino Acids

    • HLY

    • Common Amino Acids

    • R

    • Mass

    • 5587.53

    • PI

    • 10.83

    • Basic Residues

    • 10

    • Acidic Residues

    • 2

    • Hydrophobic Residues

    • 13

    • Net Charge

    • +8

    • Boman Index

    • -139.33

    • Hydrophobicity

    • -0.775

    • Aliphatic Index

    • 54.79

    • Half Life

      • Mammalian:30 hour
      • Yeast:>20 hour
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 11250

    • Absorbance 280nm

    • 239.36

    • Polar Residues

    • 12

DRAMP03635

DRAMP03635 chydropathy plot

Comments Information

    • Function

    • Lactoferricin binds to the bacterial surface and is crucial for the bactericidal functions. Has some antiviral activity against papillomavirus infection. N-terminal region shows strong antifungal activity against C.albicans. Contains two BBXB heparin-binding consensus sequences that appear to form the predominate functional GAG-binding site.

    • Tissue specificity

    • High levels are found in saliva and tears, intermediate levels in serum and plasma, and low levels in urine.

Literature Information

  • ·Literature 1

    • Title

    • Structure and association of human lactoferrin peptides with Escherichia coli lipopolysaccharide.

    • Reference

    • Antimicrob Agents Chemother. 2004 Jun;48(6):2190-2198.

    • Author

    • Chapple DS, Hussain R, Joannou CL, Hancock RE, Odell E, Evans RW, Siligardi G.
  • ·Literature 2

    • Title

    • Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent.

    • Reference

    • Antimicrob Agents Chemother. 2005 Aug;49(8):3387-3395.

    • Author

    • Hunter HN, Demcoe AR, Jenssen H, Gutteberg TJ, Vogel HJ.