General Information

    • DRAMP ID

    • DRAMP21487

    • Peptide Name

    • LL-IIIs-2

    • Sequence

    • VNWKKILGKⓍIKVⓍK

    • Sequence Length

    • 15

    • Original Sequence

    • VNWKKILGKIIKVVK

    • Source

    • Synthetic construct

Activity Information

    • 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

Structure Information

    • 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

Physicochemical Information

    • Formula

    • C₈₉H₁₅₄N₂₂O₁₇

    • Absent Amino Acids

    • ACDEFHMPQRSTY

    • Common Amino Acids

    • K

    • Mass

    • 1804.35

    • PI

    • /

    • Basic Residues

    • 5

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 6

    • Hydrophobicity

    • /

    • Polar Residues

    • 2

DRAMP21487

Literature Information

  • 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