• DRAMP ID

    • DRAMP21474
    • Peptide Name

    • peptide 8 (derived from OH-CM6)
    • Sequence

    • KFFKKLKKAVⓀKGFⓀKFAKV
    • Sequence Length

    • 20
    • Original Sequence

    • KFFKKLKKAVKKGFKKFAKV
    • Source

    • Synthetic construct
    • Biological Activity

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

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

      • [Ref.32216308] Gram-positive bacteria: Staphylococcus aureus (MIC99.9= 4 μg/mL), methicillin-resistant Staphylococcus aureus (MIC99.9= 4 μg/mL), Listeria monocytogenes (MIC99.9= 2 μg/mL);
      • Gram-negative bacteria: E.coli (MIC99.9= 8 μg/mL), Pseudomonas aeruginosa (MIC99.9= 8 μg/mL), clinically isolated drug-resistant E.coli (MIC99.9= 32 μg/mL)
    • Hemolytic Activity

      • [Ref.32216308] It has 2.7% hemolysis against red blood cells at peptide concentration of 320 μg/mL
    • 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: 11 and 15) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (11) and Ⓚ (15) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.
    • Stereochemistry

    • L
    • Secondary Structure

    • Random coils in PBS.
    • Structure Description

    • ①All the peptides were random coils in PBS but displayed varied levels of α-helicity in the presence of 30 mM SDS. ②Other stapled peptides had an α-helix content ranging from 16 to 38%, but their antibacterial activity and proteolytic stability were quite similar.
    • Helical Wheel Diagram

    • DRAMP21474 helical wheel diagram
    • Predicted Structure

    • Formula

    • C₁₂₄H₂₀₉N₃₁O₂₀
    • Absent Amino Acids

    • CDEHIMNPQRSTWY
    • Common Amino Acids

    • K
    • Mass

    • 2454.17
    • PI

    • /
    • Basic Residues

    • 8
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 9
    • Hydrophobicity

    • /
    • Polar Residues

    • 1

DRAMP21474

  • Literature 1
    • Title

    • Novel Stapling by Lysine Tethering Provides Stable and Low Hemolytic Cationic Antimicrobial Peptides
    • Reference

    • J Med Chem. 2020 Apr 23;63(8):4081-4089. doi: 10.1021/acs.jmedchem.9b02025. Epub 2020 Apr 8.
    • Author

    • Hong Li, Yuchen Hu, Qi Pu, Tong He, Qianyu Zhang, Wen Wu, Xuefeng Xia and Jinqiang Zhang