General Information

    • DRAMP ID

    • DRAMP21491

    • Peptide Name

    • LL-IIIs-5 trans

    • Sequence

    • VNⓏKKILGKⓍIKVVK

    • Sequence Length

    • 15

    • Original Sequence

    • VNWKKILGKIIKVVK

    • Source

    • Synthetic construct

Activity Information

    • Biological Activity

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

    • Comments

    • Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 100 μM.

    • Target Organism

      • [Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 1.1 μM), Bacillus subtilis (MIC = 1.3 μM), Staphylococcus aureus (MIC = 65 μM);
      • Gram-negative bacteria: E.coli (MIC = 5.5 μM), Pseudomonas aeruginosa (MIC = 80 μM);
      • Fungi: Candida albicans (MIC > 100 μM).

    • Hemolytic Activity

      • [Ref.22526241] LC50 > 100 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: 3) indicates 2-(7'-octenyl) alanine in the R configuration. ②The Ⓧ (position: 10) is 2-(4'-pentenyl) alanine in the S configuration. ③Ⓩ (3) and Ⓧ (10) are cross-linked by hydrocarbon stapling.

    • Stereochemistry

    • L, trans

    • Secondary Structure

    • ①26% α-helical content in water. ②54% α-helical content in 50% TFE. ③62% α-helical content in 8mM SDS.

    • Structure Description

    • No other descriptive information about the structure found in the literature

    • Helical Wheel Diagram

    • DRAMP21491 helical wheel diagram

    • Predicted Structure

    • There is no predicted structure for DRAMP21491.

Physicochemical Information

    • Formula

    • C₈₆H₁₅₉N₂₁O₁₇

    • Absent Amino Acids

    • ACDEFHMPQRSTWY

    • Common Amino Acids

    • K

    • Mass

    • 1759.35

    • PI

    • /

    • Basic Residues

    • 5

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 6

    • Hydrophobicity

    • /

    • Polar Residues

    • 2

DRAMP21491

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 23.

    • Author

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