• DRAMP ID

    • DRAMP03532
    • Peptide Name

    • Moricin-1 (Insects, animals)
    • Source

    • Bombyx mori (Silk moth)
    • Family

    • Belongs to the moricin family
    • Gene

    • MOR1
    • Sequence

    • AKIPIKAIKTVGKAVGKGLRAINIASTANDVFNFLKPKKRKH
    • Sequence Length

    • 42
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • Gram-negative bacteria: Escherichia coli JM109 (MIC=0.31 µM), Acinetobacter sp. NISL B-4653 (MIC=0.27 µM), Pseudomonas fluorescens IAM1179 (MIC=0.53 µM), Pseudomonas aeruginosa IAM15140 (MIC=0.81 µM);
      • Gram-positive bacteria: Bacillus subtilis IAM1107 (MIC=0.19 µM), Bacillus megaterium IAM1030 (MI=0.09 µM), Bacillus cereus IFO3457 (MIC=0.38 µM), Staphylococcus aureus ATCC6538P (MIC=0.21 µM), Staphylococcus aureus ATCC6538P (MIC=0.22 µM), Staphylococcus aureus IFO3083 (MIC=0.46 µM), Staphylococcus xylosus IAM1312 (MIC=0.27 µM), Staphylococcus epidermidis IFO12993 (MIC=0.18 µM), Streptococcus pyogenes ATCC21547 (MIC=0.25 µM).
    • Hemolytic Activity

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

      • Not included yet
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Free
    • Nonterminal Modifications and Unusual Amino Acids

    • Free
    • Stereochemistry

    • L
    • Structure

    • Alpha helix (1 helices; 30 residues)
    • Structure Description

    • The solution structure reveals an unique structure comprising of a long alpha-helix containing eight turns along nearly the full length of the peptide except for four N-terminal residues and six C-terminal residues. The electrostatic surface map shows that the N-terminal segment of the alpha-helix, residues 5-22, is an amphipathic alpha-helix with a clear separation of hydrophobic and hydrophilic faces, and that the C-terminal segment o
    • Helical Wheel Diagram

    • DRAMP03532 helical wheel diagram
    • PDB ID

    • 1KV4 resolved by NMR.
  • 1KV4-> 
    • Predicted Structure

    • Formula

    • C208H358N62O51
    • Absent Amino Acids

    • CEMQWY
    • Common Amino Acids

    • K
    • Mass

    • 4543.52
    • PI

    • 11.36
    • Basic Residues

    • 12
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 18
    • Net Charge

    • +11
    • Boman Index

    • -55.43
    • Hydrophobicity

    • -0.21
    • Aliphatic Index

    • 100
    • Half Life

      • Mammalian:4.4 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 9

DRAMP03532

DRAMP03532 chydropathy plot
    • Function

    • Has antibacterial activity against Gram-positive and Gram-negative bacteria. Probably acts by disturbing membrane functions with its amphipathic structure.
  • ·Literature 1
    • Title

    • Moricin, a novel type of antibacterial peptide isolated from the silkworm, Bombyx mori.
    • Reference

    • J Biol Chem. 1995 Dec 15;270(50):29923-29927.
    • Author

    • Hara S, Yamakawa M.
  • ·Literature 2
    • Title

    • Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori.
    • Reference

    • FEBS Lett. 2002 May 8;518(1-3):33-38.
    • Author

    • Hemmi H, Ishibashi J, Hara S, Yamakawa M.