• DRAMP ID

    • DRAMP21482
    • Peptide Name

    • S-6K-F17
    • Sequence

    • KKKKKKAAFⓍAWAⓍFAA
    • Sequence Length

    • 17
    • Original Sequence

    • KKKKKKAAFAAWAAFAA
    • Source

    • Synthetic construct
    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram-
    • Comments

    • Function: Antibacterial activity against Gram-negative bacteria. No experiments about antibacterial activity against Gram-positive bacteria are recorded.
    • Target Organism

      • [Ref.29275987] Gram-negative bacteria: E. coli (MIC= 1.0 μM)
    • Hemolytic Activity

      • [Ref.29275987] MHC = 3.8 μM against human red blood cells. Note: Minimum hemolytic concentration (MHC) is the minimum peptide concentration at which red blood cells undergo > 2% hemolysis.
    • 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: 10 and 14) in sequence indicates 2-(4'-pentenyl) alanine. ②Ⓧ (10) and Ⓧ (14) are cross-linked by hydrocarbon stapling.
    • Stereochemistry

    • L
    • Secondary Structure

    • ①Random coils with only a small amount of helical structure in aqueous buffer. ②α-helix in SDS detergent micelles.
    • Structure Description

    • ①Similarly, the stapled peptide, S-6K-F17 is predominantly random coil in aqueous buffer with only a small amount of helical structure despite the presence of the staple - a feature likely due to the large stretch of non-helical Lys residues that flank the stapled portion of the sequence. ②As expected, in detergent micelles S-6K-F17 adopts a helical structure, paralleling the unstapled peptide.
    • Helical Wheel Diagram

    • DRAMP21482 helical wheel diagram
    • Predicted Structure

    • Formula

    • C₉₇H₁₅₄N₂₄O₁₈
    • Absent Amino Acids

    • CDEGHILMNPQRSTVY
    • Common Amino Acids

    • AK
    • Mass

    • 1944.44
    • PI

    • /
    • Basic Residues

    • 6
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 9
    • Hydrophobicity

    • 2.35
    • Polar Residues

    • 0

DRAMP21482

  • Literature 1
    • Title

    • Influence of hydrocarbon-stapling on membrane interactions of synthetic antimicrobial peptides
    • Reference

    • Bioorg Med Chem. 2018 Mar 15;26(6):1189-1196. doi: 10.1016/j.bmc.2017.10.020. Epub 2017 Oct 21.
    • Author

    • Tracy A Stone, Gregory B Cole, Huong Q Nguyen, Simon Sharpe, Charles M Deber