• DRAMP ID

    • DRAMP21337
    • Peptide Name

    • BMAP-27 (Bovine, mammals, animals)
    • Source

    • Bos taurus (Bovine)
    • Family

    • Belongs to the cathelicidin family
    • Gene

    • CATHL6
    • Sequence

    • GRFKRFRKKFKKLFKKLSPVIPLLHL
    • Sequence Length

    • 26
    • Evidence code

    • Protein level
    • Biological Activity

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

      • [Ref.31226350] Gram-positive bacteria:Staphylococcus aureus (MIC=1-2 μM);
      • Gram-negative bacteria: Escherichia coli (MIC=2-4 μM)
    • Hemolytic Activity

      • [Ref.31226350] 50% hemolysis at 75 μM for human red blood cells
    • Cytotoxicity

      • [Ref.31226350] The CC50 values which represent peptide concentration (μM) inducing 50% cytotoxicity to human cancer cell lines of BMAP-27 on MDA361 and A549 are 4.2 μM and 5.3 μM. DETAILED DATA: ①The cell viability of MDA-361 induced by BMAP-27 is 100%, 100%, 98.9%, 97.7%, 87.6%, 59.8%, 34.7%, 12.4%, 10.3%, 8.3% and 9.4% at peptide concentrations of 0.1, 0.2, 0.4, 0.8, 1.6, 3.2, 6.4, 13, 25, 50 and 100 μM. ②The cell viability of A549 induced by BMAP-27 is 100%, 99.1%, 97.7%, 94.7%, 74.5%, 41.4%, 24.4%, 11.3%, 9.7%, 10.3% and 7.4% at peptide concentrations of 0.1, 0.2, 0.4, 0.8, 1.6, 3.2, 6.4, 13, 25, 50 and 100 μM.
    • Binding Target

    • N/A
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Amidation
    • Other Modifications and Unusual Amino Acids

    • None
    • Stereochemistry

    • L
    • Structure

    • 73% α-helix in 50% TFE/H2O
    • Structure Description

    • An α-helix occurred from Arg2 to Leu17 in the N-terminal region and a short α-helix is observed from Leu23 to Leu26 in the Cterminal region; the two regions are connected with a flexible region containing two proline residues.
    • DRAMP21337 helical wheel diagram
    • Formula

    • C158H262N44O28
    • Absent Amino Acids

    • ACDEMNQTWY
    • Common Amino Acids

    • K
    • Mass

    • 3226.1
    • PI

    • 12.32
    • Basic Residues

    • 11
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 11
    • Boman Index

    • -4525
    • Hydrophobicity

    • -36.54
    • Aliphatic Index

    • 101.15
    • Half Life

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

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 2

DRAMP21337

DRAMP21337 chydropathy plot
    • Function

    • Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.
  • Literature 1
    • Title

    • Structural analysis and mode of action of BMAP-27, a cathelicidin-derived antimicrobial peptide
    • Reference

    • Peptides. 2019 Jun 18;118:170106. doi: 10.1016/j.peptides.2019.170106.
    • Author

    • Yang S, Lee CW, Kim HJ, Jung HH, Kim JI, Shin SY, Shin SH