• DRAMP ID

    • DRAMP29033
    • Peptide Name

    • Stripe-based foldamer peptide 5
    • Sequence

    • KLLKKⓏGKLLKKⓍGKLLKKAG
    • Sequence Length

    • 21
    • Original Sequence

    • KLLKKAGKLLKKAGKLLKKAG
    • Source

    • Synthetic construct
    • Biological Activity

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

    • Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. It is a helical foldmer peptide based on "Stripe" (an AMP manually designed) by introducing a hydrocarbon stapling. The peptide showed weaker activity than Stripe.
    • Target Organism

      • [Ref.33369262] Gram-positive bacteria: Staphylococcus aureus NBRC13276 (MIC = 25 μM) ;
      • Gram-negative bacteria: Escherichia coli DH5α (MIC = 6.25 μM), Pseudomonas aeruginosa NBRC13275 (MIC = 12.5 μM), multidrug-resistant Pseudomonas aeruginosa ATCCBAA-2111 (MDRP) (MIC = 25 μM)
    • Hemolytic Activity

      • [Ref.33369262] It exhibits hemolysis at 1.56 μM agasint human red blood cells.
    • Cytotoxicity

    • No cytotoxicity information found in the reference(s) presented
    • Linear/Cyclic

    • Cyclic (Stapled)
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Free
    • Special Amino Acid and Stapling Position

    • ①The Ⓩ (position: 6) in sequence denotes (R)-(7-octenyl)alanine. ②The Ⓧ (position: 13) in sequence denotes (S)-(4-pentenyl)alanine. ③ Ⓩ (6) and Ⓧ (13) are cross-linked by side-stapling through a undec-4-enyl staple.
    • Stereochemistry

    • L
    • Secondary Structure

    • α-Helix content = 34% in 20 mM phosphate buffered saline (PBS) solution (pH 7.4), with 1% sodium dodecyl sulfate
    • Structure Description

    • [Ref.33369262] As shown in Figure 2, peptides 2, 3, 4 and 5 showed negative maxima at around 208 and 222nm, which suggests that they formed stable α-helical structures, similar to Stripe.
    • Helical Wheel Diagram

    • DRAMP29033 helical wheel diagram
    • Predicted Structure

    • Formula

    • C₁₁₇H₂₁₉N₃₁O₂₁
    • Absent Amino Acids

    • CDEFHIMNPQRSTVWY
    • Common Amino Acids

    • K
    • Mass

    • 2396.18
    • PI

    • /
    • Basic Residues

    • 9
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 7
    • Hydrophobicity

    • /
    • Polar Residues

    • 3

DRAMP29033

  • Literature 1
    • Title

    • Rational Design of Helix-Stabilized Antimicrobial Peptide Foldamers Containing α,α-Disubstituted Amino Acids or Side-Chain Stapling
    • Reference

    • Chempluschem. 2020 Dec;85(12):2731-2736. doi: 10.1002/cplu.202000749.
    • Author

    • Motoharu Hirano, Chihiro Saito, Chihiro Goto, Hidetomo Yokoo, Ryuji Kawano, Takashi Misawa, Yosuke Demizu