• DRAMP ID

    • DRAMP21567
    • Peptide Name

    • MP1S-D8N
    • Sequence

    • IDWKKⓍLNAⓍKQIL
    • Sequence Length

    • 14
    • Original Sequence

    • IDWKKLLDAAKQIL
    • Source

    • Synthetic construct
    • Biological Activity

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

    • Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.
    • Target Organism

      • [Ref.29075946] Gram-positive bacteria: Bacillus subtilis (MIC = 0.8 μg/mL), Staphylococcus aureus (MIC = 0.8 μg/mL), Staphylococcus epidermidis (MIC = 37.5 μg/mL);
      • Gram-negative bacteria: Escherichia coli (MIC = 50 μg/mL), Shigella dysenteriae (MIC = 100 μg/mL), Salmonella typhimurium (MIC > 100 μg/mL), Klebsiella pneumoniae (MIC = 37.5 μg/mL), Pseudomonas aeruginosa (MIC ≥ 100 μg/mL)
    • Hemolytic Activity

      • [Ref.29075946] It has 16.3% hemolysis against human red blood cells at 12.5 μM and 37.8% hemolysis at 25 μM.
    • Cytotoxicity

    • No cytotoxicity information found in the reference(s) presented
    • Linear/Cyclic

    • Cyclic (Stapled)
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Amidation
    • Special Amino Acid and Stapling Position

    • ①The Ⓧ (position: 6 and 10) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (6) and Ⓧ (10) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.
    • Stereochemistry

    • L
    • Secondary Structure

    • 89.4% α-helical content in a 25 mM potassium phosphate buffer solution at 20℃
    • Structure Description

    • ①Helical contents of all stapled analogues were increased by more than a three-fold compared to their unmodified counterpart, MP1. ②MP1S-D8N and MP1S-Q12K showed slightly lower helical contents (89.4% and 81.8, respectively).
    • Helical Wheel Diagram

    • DRAMP21567 helical wheel diagram
    • Predicted Structure

    • There is no predicted structure for DRAMP21567.
    • Formula

    • C₈₃H₁₃₈N₂₁O₁₈
    • Absent Amino Acids

    • CEFGHMPRSTVY
    • Common Amino Acids

    • K
    • Mass

    • 1720.14
    • PI

    • /
    • Basic Residues

    • 3
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 6
    • Hydrophobicity

    • /
    • Polar Residues

    • 1

DRAMP21567

  • Literature 1
    • Title

    • Antimicrobial activity and stability of stapled helices of polybia-MP1
    • Reference

    • Arch Pharm Res. 2017 Dec;40(12):1414-1419. doi: 10.1007/s12272-017-0963-5. Epub 2017 Oct 26.
    • Author

    • Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim