• DRAMP ID

    • DRAMP21487
    • Peptide Name

    • LL-IIIs-2
    • Sequence

    • VNWKKILGKⓍIKVⓍK
    • 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 = 0.9 μM), Bacillus subtilis (MIC = 1.2 μM), Staphylococcus aureus (MIC = 20.3 μM);
      • Gram-negative bacteria: E.coli (MIC = 8.8 μM), Pseudomonas aeruginosa (MIC = 86.7 μM);
      • Fungi: Candida albicans (MIC = 100 μM).
    • Hemolytic Activity

      • [Ref.22526241] LC50 = 69 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: 10 and 14) indicates 2-(4'-pentenyl) alanine in the S configuration. ②Ⓧ (10) and Ⓧ (14)are cross-linked by hydrocarbon stapling.
    • Stereochemistry

    • L
    • Secondary Structure

    • ①31% α-helical content in water. ②51% α-helical content in 50% TFE. ③58% α-helical content in 8mM SDS.
    • Structure Description

    • For the LL-IIIs-2 analog, the helical content increment is slightly higher (8 %).
    • Helical Wheel Diagram

    • DRAMP21487 helical wheel diagram
    • Predicted Structure

  • 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 19.
    • Author

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