General Information

    • DRAMP ID

    • DRAMP03535

    • Peptide Name

    • Lebocin-1/2 (Pro-rich; Insects, animals)

    • Source

    • Bombyx mori (Silk moth)

    • Family

    • Belongs to the lebocin family

    • Gene

    • Not found

    • Sequence

    • DLRFLYPRGKLPVPTPPPFNPKPIYIDMGNRY

    • Sequence Length

    • 32

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

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

    • Target Organism

      • Gram-negative bacteria: Acinetobacter sp. NISL B-4653, Escherichia coli HB1ll, Pseudomonas fluorescens IAM1179;
      • Gram-positive bacterium: Staphylococcus aureus ATCC6538P.

    • 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

    • Rich

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP03535 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP03535.

Physicochemical Information

    • Formula

    • C179H271N45O43S

    • Absent Amino Acids

    • ACEHQSW

    • Common Amino Acids

    • P

    • Mass

    • 3773.46

    • PI

    • 9.82

    • Basic Residues

    • 5

    • Acidic Residues

    • 2

    • Hydrophobic Residues

    • 8

    • Net Charge

    • +3

    • Boman Index

    • -50.74

    • Hydrophobicity

    • -0.669

    • Aliphatic Index

    • 70

    • Half Life

      • Mammalian:1.1 hour
      • Yeast:3 min
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 4470

    • Absorbance 280nm

    • 144.19

    • Polar Residues

    • 8

DRAMP03535

DRAMP03535 chydropathy plot

Comments Information

    • Function

    • Antibacterial peptide.

    • Tissue specificity

    • Hemolymph. Produced in fat body.

    • Induction

    • By bacterial infection.

    • PTM

    • O-glycosylation is important for the antibacterial activity of lebocin, O-linked glycan structure is a disaccharide (Gal-GalNAc) in case of lebocin 1 and a monosaccharide (GalNAc) in case of lebocin 2.

Literature Information

  • ·Literature 1

    • Title

    • A novel antibacterial peptide family isolated from the silkworm, Bombyx mori.

    • Reference

    • Biochem J. 1995 Sep 1;310 (Pt 2):651-656.

    • Author

    • Hara S, Yamakawa M.
  • ·Literature 2

    • Title

    • cDNA cloning and gene expression of lebocin, a novel member of antibacterial peptides from the silkworm, Bombyx mori.

    • Reference

    • Biochem Biophys Res Commun. 1995 Sep 5;214(1):271-278.

    • Author

    • Chowdhury S, Taniai K, Hara S, Kadono-Okuda K, Kato Y, Yamamoto M, Xu J, Choi SK, Debnath NC, Choi HK, et al.