• • 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

• • UniProt Entry

  • P82818

• • Protein Existence

  • Protein level

• • Biological Activity

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

• • Target Organism

  • • Gram-negative bacteria:

      Target Organism	Activity
      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:

      Target Organism	Activity
      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

  • 

• • PDB ID

  • 1KV4 resolved by NMR.

• Predicted Structure

• There is no predicted structure for DRAMP03532.

DRAMP03532

• • 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.

• • Pubmed ID

  • 8530391

• • 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.

• • Pubmed ID

  • 11997013

• • Reference

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

• • Author

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