General Information

    • DRAMP ID

    • DRAMP01095

    • Peptide Name

    • Bombinin-like peptide 2 (Contains: Bombinin H2; toads, amphibians, animals)

    • Source

    • Bombina variegata (Yellow-bellied toad)

    • Family

    • Belongs to the bombinin family

    • Gene

    • Not found

    • Sequence

    • GIGASILSAGKSALKGFAKGLAEHFAN

    • Sequence Length

    • 27

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial

    • Target Organism

    • No MICs found in DRAMP database

    • Hemolytic Activity

      • [Ref:10333736]Non-hemolytic activity

    • 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

    • Not found

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP01095 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP01095.

Physicochemical Information

    • Formula

    • C118H191N33O34

    • Absent Amino Acids

    • CDMPQRTVWY

    • Common Amino Acids

    • A

    • Mass

    • 2616.02

    • PI

    • 9.7

    • Basic Residues

    • 4

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 13

    • Net Charge

    • +3

    • Boman Index

    • 1.16

    • Hydrophobicity

    • 0.389

    • Aliphatic Index

    • 94.44

    • Half Life

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

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 9

DRAMP01095

DRAMP01095 chydropathy plot

Comments Information

    • Function

    • Bombinin-like peptide 2 has antimicrobial activity, but no hemolytic activity. Preliminary evidence indicates that this peptide does not lyse and thus kill the bacteria by its antimicrobial activity. Bombinin H2 has antibacterial and hemolytic activity.

    • Tissue specificity

    • Expressed by the skin glands.

Literature Information

  • ·Literature 1

    • Title

    • Antimicrobial peptides from amphibian skin: what do they tell us?

    • Reference

    • Biopolymers. 1998;47(6):435-450.

    • Author

    • Simmaco M, Mignogna G, Barra D.
  • ·Literature 2

    • Title

    • Antibacterial and haemolytic peptides containing D-alloisoleucine from the skin of Bombina variegata.

    • Reference

    • EMBO J. 1993 Dec;12(12):4829-4832.

    • Author

    • Mignogna G, Simmaco M, Kreil G, Barra D.