• DRAMP ID

    • DRAMP21486
    • Peptide Name

    • LL-IIIs-1
    • Sequence

    • VNWKKⓍLGKⓍIKVVK
    • Sequence Length

    • 15
    • Original Sequence

    • VNWKKILGKIIKVVK
    • Source

    • Synthetic construct
    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal
    • Comments

    • Function: Antibacterial activity against Gram-positive and Gram-negative bacteria and Antifungal activity against Candida albicans.
    • Target Organism

      • [Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 0.7 μM), Bacillus subtilis (MIC = 0.8 μM), Staphylococcus aureus (MIC = 12.5 μM);
      • Gram-negative bacteria: E.coli (MIC = 4.4 μM), Pseudomonas aeruginosa (MIC = 78.7 μM);
      • Fungi: Candida albicans (MIC = 100 μM).
    • Hemolytic Activity

      • [Ref.22526241] LC50 = 31.3 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.
    • 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: 6 and 10) indicates 2-(4'-pentenyl) alanine in the S configuration. ②Ⓧ (6) and Ⓧ (10) are cross-linked by hydrocarbon stapling.
    • Stereochemistry

    • L
    • Secondary Structure

    • ①20% α-helical content in water. ②55% α-helical content in 50% TFE. ③55% α-helical content in 8mM SDS.
    • Structure Description

    • It seems that the staple in the central part of the LL-IIIs-1 analog that crosslink the bend of the α-helix on its concave site around the Gly8 residue resulted in slight helix destabilization.
    • Helical Wheel Diagram

    • DRAMP21486 helical wheel diagram
    • Predicted Structure

    • Formula

    • C₈₈H₁₅₂N₂₂O₁₇
    • Absent Amino Acids

    • ACDEFHMPQRSTY
    • Common Amino Acids

    • K
    • Mass

    • 1790.32
    • PI

    • /
    • Basic Residues

    • 5
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 6
    • Hydrophobicity

    • /
    • Polar Residues

    • 2

DRAMP21486

  • Literature 1
    • Title

    • Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera
    • Reference

    • Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 18.
    • Author

    • Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský