• DRAMP ID

    • DRAMP21528
    • Peptide Name

    • Mag(i+4)15(H7K)
    • Sequence

    • GIGKFLKSAKKFGKAⓍVGEⓍJNS
    • Sequence Length

    • 23
    • Original Sequence

    • GIGKFLHSAKKFGKAFVGEIMNS
    • 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.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 6.20 μg/mL), Bacillus cereus ATCC 14579 (MIC = 5.21 μg/mL);
      • Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.60 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 2.69 μg/mL)
    • Hemolytic Activity

      • [Ref.31427820] It has 3.1% hemolysis against human red blood cells at 25 μg/mL.
    • 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: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.
    • Stereochemistry

    • L
    • Secondary Structure

    • α-helix in potassium phosphate buffer.
    • Structure Description

    • No other descriptive information about the structure found in the literature
    • Helical Wheel Diagram

    • DRAMP21528 helical wheel diagram
    • Predicted Structure

    • There is no predicted structure for DRAMP21528.
    • Formula

    • C₁₁₄H₁₈₉N₂₉O₂₉
    • Absent Amino Acids

    • CDHMPQRTWY
    • Common Amino Acids

    • K
    • Mass

    • 2429.94
    • PI

    • /
    • Basic Residues

    • 5
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 7
    • Hydrophobicity

    • /
    • Polar Residues

    • 7

DRAMP21528

  • Literature 1
    • Title

    • Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice
    • Reference

    • Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.
    • Author

    • Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky