• DRAMP ID

    • DRAMP21564
    • Peptide Name

    • KRR
    • Sequence

    • KⓍWRJⓍR
    • Sequence Length

    • 7
    • Original Sequence

    • /
    • 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.30361948] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 6.3 μM), Staphyolococcus aureus ATCC 6538p (MIC = 3.2 μM), Staphylococcus epidermidis ATCC 12228 (MIC = 12.5 μM);
      • Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 12.5 μM), Shigella dysenteriae ATCC 9752 (MIC = 25 μM), Salmonella typhimurium ATCC 14028 (MIC = 50 μM), Klebsiella pneumoniae ATCC 10031 (MIC = 18.8 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 37.5 μM)
    • Hemolytic Activity

      • [Ref.30361948] It has 1.8% hemolysis against human red blood cells at 25 μM and 5.6% hemolysis at 50 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 J (position: 5) in sequence is norleucine. ②The Ⓧ (position: 2 and 6) indicates (S)-α-methyl, α-pentenylglycine. ③Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.
    • Stereochemistry

    • L
    • Secondary Structure

    • α-helix in a 25 mM potassium phosphate solution (pH 6.5).
    • Structure Description

    • All analogs displayed similar CD spectra to that of KKK, having two minima near 208 and 222 nm and a maximum near 190nm, which are characteristic of α-helices.
    • Helical Wheel Diagram

    • DRAMP21564 helical wheel diagram
    • Predicted Structure

    • There is no predicted structure for DRAMP21564.
    • Formula

    • C₄₉H₈₁N₁₅O₈
    • Absent Amino Acids

    • ACDEFGHILMNPQSTVY
    • Common Amino Acids

    • RX
    • Mass

    • 1008.28
    • PI

    • /
    • Basic Residues

    • 3
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 1
    • Hydrophobicity

    • /
    • Polar Residues

    • 0

DRAMP21564

  • Literature 1
    • Title

    • Effects of lysine-to-arginine substitution on antimicrobial activity of cationic stapled heptapeptides
    • Reference

    • Arch Pharm Res. 2018 Nov;41(11):1092-1097. doi: 10.1007/s12272-018-1084-5. Epub 2018 Oct 25.
    • Author

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