• DRAMP ID

    • DRAMP21543
    • Peptide Name

    • Esc(i+4)1,14(A7K)
    • Sequence

    • GⓍFSKⓍKGKKIKNLⓍISGⓍKG
    • Sequence Length

    • 21
    • Original Sequence

    • GIFSKLAGKKIKNLLISGLK
    • 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 = 50 μg/mL), Bacillus cereus ATCC 14579 (MIC = 12.5 μg/mL);
      • Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.56 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 1.56 μg/mL)
    • Hemolytic Activity

      • [Ref.31427820] It has 2.5% 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: 2, 6, 15 and 19) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (2) and Ⓧ (6), Ⓧ (15) and Ⓧ (19) are cross-linked by hydrocarbon stapling respectively.
    • 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

    • DRAMP21543 helical wheel diagram
    • Predicted Structure

  • 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