• DRAMP ID

    • DRAMP21619
    • Peptide Name

    • sWWSP
    • Sequence

    • PLIⓀLRLⒹRGQF
    • Sequence Length

    • 12
    • Original Sequence

    • PLILLRLLRGQF
    • 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.28921993] Gram-positive bacteria: Staphylococcus aureus (MIC > 256 μg/mL), Enterococcus faecalis (MIC > 256 μg/mL);
      • Gram-negative bacteria: Escherichia coli (MIC > 256 μg/mL), Pseudomonas aeruginosa (MIC > 256 μg/mL)
    • Hemolytic Activity

      • [Ref.28921993] It has 4.0%, 4.8%, 4.6%, 4.2% and 7.0% hemolysis against human red blood cells at 15, 20, 25, 30 and 40 μg/ml.
    • Cytotoxicity

      • [Ref.28921993] The toxicity of sWWSP toward HEK293 and HeLa cells is much less than nonaarginine (R9) by use of flow cytometry and the peptide doesn't show any cytotoxicity at 2 μM.
    • Linear/Cyclic

    • Cyclic (Stapled)
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Amidation
    • Special Amino Acid and Stapling Position

    • Ⓚ (4) and Ⓓ (8) are cross-linked by lactam stapling through the polar amide bond of a lactam bridge.
    • Stereochemistry

    • L
    • Secondary Structure

    • ①α-helix in aqueous solutions [pure water (H₂O), phosphate buffer (PB, 10 mM), and phosphate buffer with high salt (NaF, 100 mM)]. ②43% average α-helix content in various membranes environments [38% in POPC; 58% in POPC/POPG(3:1); 47% in POPC:lysoPC(9:1);
    • Structure Description

    • On the other hand, sWWSP and sMAP-1 assumed an α-helical conformation in aqueous solution, in contrast to their unstructured linear countparts.
    • Helical Wheel Diagram

    • DRAMP21619 helical wheel diagram
    • Predicted Structure

    • There is no predicted structure for DRAMP21619.
    • Formula

    • C₆₉H₁₁₇N₁₉O₁₃
    • Absent Amino Acids

    • ACEHMNSTVWY
    • Common Amino Acids

    • L
    • Mass

    • 1420.8
    • PI

    • /
    • Basic Residues

    • 3
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 5
    • Hydrophobicity

    • /
    • Polar Residues

    • 1

DRAMP21619

  • Literature 1
    • Title

    • Lactam-Stapled Cell-Penetrating Peptides: Cell Uptake and Membrane Binding Properties.
    • Reference

    • J Med Chem. 2017 Oct 12;60(19):8071-8082. doi: 10.1021/acs.jmedchem.7b00813. Epub 2017 Sep 26.
    • Author

    • Marco J Klein, Samuel Schmidt, Parvesh Wadhwani, Jochen Bürck, Johannes Reichert, Sergii Afonin, Marina Berditsch, Tim Schober, Roland Brock, Manfred Kansy, Anne S Ulrich