General Information

    • DRAMP ID

    • DRAMP03015

    • Peptide Name

    • Bombolitin-8 (Insects, animals)

    • Source

    • Bombus lapidarius (Red-tailed bumblebee) (Apis lapidaria)

    • Family

    • Belongs to the MCD family Bombolitin subfamily

    • Gene

    • Not found

    • Sequence

    • LKLKSILGKLGVILSHLNK

    • Sequence Length

    • 19

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Antifungal

    • Target Organism

    • No MICs found in DRAMP database

    • 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

    • Not found

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP03015 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP03015.

Physicochemical Information

    • Formula

    • C97H176N26O23

    • Absent Amino Acids

    • ACDEFMPQRTWY

    • Common Amino Acids

    • L

    • Mass

    • 2074.62

    • PI

    • 10.48

    • Basic Residues

    • 5

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 9

    • Net Charge

    • +5

    • Boman Index

    • 4.98

    • Hydrophobicity

    • 0.595

    • Aliphatic Index

    • 179.47

    • Half Life

      • Mammalian:5.5 hour
      • Yeast:3 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 5

DRAMP03015

DRAMP03015 chydropathy plot

Comments Information

    • Function

    • Mast cell degranulating peptide. May also display antibacterial and antifungal activities (By similarity).

    • Tissue specificity

    • Expressed by the venom gland.

Literature Information

  • ·Literature 1

    • Title

    • Mass spectrometry strategies for venom mapping and peptide sequencing from crude venoms: case applications with single arthropod specimen.

    • Reference

    • Toxicon. 2006 May;47(6):676-687.

    • Author

    • Favreau P, Menin L, Michalet S, Perret F, Cheneval O, Stöcklin M, Bulet P, Stöcklin R.