General Information

    • DRAMP ID

    • DRAMP02840

    • Peptide Name

    • Lactoferricin B (Lfcin B; mammals, animals)

    • Source

    • Bos taurus (Bovine)

    • Family

    • Belongs to the transferrin family

    • Gene

    • LTF

    • Sequence

    • FKCRRWQWRMKKLGAPSITCVRRAF

    • Sequence Length

    • 25

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-

    • Target Organism

      • [Ref.8980754] Gram-negative bacteria: Escherichia coli L361 (MIC=4 µM or 12.5 µg/ml), Salmonella Salford (MIC=4 µM or 12.5 µg/ml), Escherichia coli O:9 (MIC=6 µM or 18.8 µg/ml), Pseudomonas fluorescens (MIC=10 µM or 31.3 µg/ml) ;
      • Gram-positive bacteria: Listeria monocytogenes (MIC=2 µM or 6.3 µg/ml), Staphylococcus aureus (MIC=6 µM or 18.8 µg/ml), Bacillus cereus (MIC=6 µM or 18.8 µg/ml)

    • Hemolytic Activity

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

    • Cytotoxicity

    • No cytotoxicity information found in the reference(s) presented

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Cyclic

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Free

    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bond between Cys3 and Cys20.

    • Stereochemistry

    • L

    • Structure

    • Beta strand (4 strands; 8 residues)

    • Structure Description

    • Residues 7-9 form beta1 and residues 17-19 form beta2 (in membrane). This contrasts with X-ray structure where residues 1-13 is helical. Thus, this peptide appears to be able to adopt a different conformation depending on environmental conditions. disulfide bond is not required for the antimicrobial potency.

    • Helical Wheel Diagram

    • DRAMP02840 helical wheel diagram

    • PDB ID

    • 1LFC resolved by NMR.
  • 1LFC-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP02840.

Physicochemical Information

    • Formula

    • C141H226N46O29S3

    • Absent Amino Acids

    • DEHNY

    • Common Amino Acids

    • R

    • Mass

    • 3125.82

    • PI

    • 11.84

    • Basic Residues

    • 8

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 9

    • Net Charge

    • +8

    • Boman Index

    • -68.79

    • Hydrophobicity

    • -0.576

    • Aliphatic Index

    • 50.8

    • Half Life

      • Mammalian:1.1 hour
      • Yeast:3 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 11125

    • Absorbance 280nm

    • 463.54

    • Polar Residues

    • 5

DRAMP02840

DRAMP02840 chydropathy plot

Comments Information

    • Function

    • Lactoferricin B function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites.

    • Activity regulation

    • Inhibited by PMSF and Pefabloc.

    • PTM

    • Contains one disulfide bond 3-20

Literature Information

  • ·Literature 1

    • Title

    • Antibacterial activity in bovine lactoferrin-derived peptides.

    • Reference

    • Antimicrob Agents Chemother. 1997 Jan;41(1):54-59.

    • Author

    • Hoek KS, Milne JM, Grieve PA, Dionysius DA, Smith R.
  • ·Literature 2

    • Title

    • Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin.

    • Reference

    • Biochemistry. 1998 Mar 24;37(12):4288-4298.

    • Author

    • Hwang PM, Zhou N, Shan X, Arrowsmith CH, Vogel HJ.
  • ·Literature 3

    • Title

    • Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin.

    • Reference

    • J Appl Bacteriol. 1992 Dec;73(6):472-9.

    • Author

    • Bellamy W, Takase M, Wakabayashi H, Kawase K, Tomita M.1992