• DRAMP ID

    • DRAMP21582
    • Peptide Name

    • S3
    • Sequence

    • KⓍWKLⓍK
    • 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

      • Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 25 μg/mL), Staphylcocccus aureus ATCC 6538p (MIC = 25 μg/mL), Staphylcococcus epidermis ATCC 12228 (MIC = 100 μg/mL);
      • Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μg/mL), Shigella dysentariae ATCC 9752 (MIC = 50 μg/mL), Salmonella typhimurium ATCC 14028 (MIC = 100 μg/mL), Klebsiella pneumonia ATCC 10031 (MIC = 50 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 75 μg/mL)
    • Hemolytic Activity

      • It has <1% hemolysis against human red blood cells at 6.3 μM and <1% hemolysis at 12.5 μM.
    • Cytotoxicity

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

    • Cyclic (Stapled)
    • N-terminal Modification

    • Acetylation
    • C-terminal Modification

    • Amidation
    • Special Amino Acid and Stapling Position

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

    • L
    • Secondary Structure

    • Stable α-helix in a 25 mM potassium phosphate buffer solution at 20 ℃
    • Structure Description

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

    • DRAMP21582 helical wheel diagram
    • Predicted Structure

    • There is no predicted structure for DRAMP21582.
    • Formula

    • C₄₉H₈₁N₁₁O₈
    • Absent Amino Acids

    • ACDEFGHIMNPQRSTVY
    • Common Amino Acids

    • K
    • Mass

    • 952.26
    • PI

    • /
    • Basic Residues

    • 3
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 2
    • Hydrophobicity

    • /
    • Polar Residues

    • 0

DRAMP21582

  • Literature 1
    • Title

    • Antimicrobial and Hemolytic Activity of Stapled Heptapeptide Dimers
    • Reference

    • B KOREAN CHEM SOC. 2016 Aug;37(8)1199-1203. doi: 10.1002/bkcs.10839.
    • Author

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