General Information

    • DRAMP ID

    • DRAMP21482

    • Peptide Name

    • S-6K-F17

    • Sequence

    • KKKKKKAAFⓍAWAⓍFAA

    • Sequence Length

    • 17

    • Original Sequence

    • KKKKKKAAFAAWAAFAA

    • Source

    • Synthetic construct

Activity Information

    • 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= 1.0 μM)

    • Hemolytic Activity

      • [Ref.29275987] MHC = 3.8 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

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) in sequence indicates 2-(4'-pentenyl) alanine. ②Ⓧ (10) and Ⓧ (14) are cross-linked by hydrocarbon stapling.

    • Stereochemistry

    • L

    • Secondary Structure

    • ①Random coils with only a small amount of helical structure in aqueous buffer. ②α-helix in SDS detergent micelles.

    • Structure Description

    • ①Similarly, the stapled peptide, S-6K-F17 is predominantly random coil in aqueous buffer with only a small amount of helical structure despite the presence of the staple - a feature likely due to the large stretch of non-helical Lys residues that flank the stapled portion of the sequence. ②As expected, in detergent micelles S-6K-F17 adopts a helical structure, paralleling the unstapled peptide.

    • Helical Wheel Diagram

    • DRAMP21482 helical wheel diagram

    • Predicted Structure

Literature Information

  • 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