• DRAMP ID

    • DRAMP21484
    • Peptide Name

    • S-6K-F17-3G
    • Sequence

    • KKKKKKAGFⓍAWGⓍFGA
    • 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= 4.2 μM)
    • Hemolytic Activity

      • [Ref.29275987] MHC = 128 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

    • Lack of significant structure
    • Structure Description

    • Substitutions with polar, known 'helix-breaker' Gly residues led to losses in helical character until finally the peptide containing 3 Gly and 1 Asn (S-6K-F17-3GN) shows a severe loss in helical structure
    • Helical Wheel Diagram

    • DRAMP21484 helical wheel diagram
    • Predicted Structure

  • 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