• DRAMP ID

    • DRAMP21503
    • Peptide Name

    • C-MP1-2
    • Sequence

    • IⓀWKKLLⒼAAKQIL
    • Sequence Length

    • 14
    • Original Sequence

    • IDWKKLLDAAKQIL
    • Source

    • Synthetic construct
    • Biological Activity

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

    • Function: Antibacterial activity against Gram-positive bacteria. Antibacterial activity against Gram-negative bacteria is not so evident.
    • Target Organism

      • [Ref.28833783] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 256 μM), Bacillus subtilis ATCC 23857 (MIC = 128 μM);
      • Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 128 μM), Pseudomonas aeruginosa ATCC 27853 (No antimicrobial activity)
    • Hemolytic Activity

      • [Ref.28833783] No hemolytic information found.
    • Cytotoxicity

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

    • Cyclic (Stapled)
    • N-terminal Modification

    • Acetylation
    • C-terminal Modification

    • Amidation
    • Special Amino Acid and Stapling Position

    • ①The Ⓚ (position: 2) is lysine with the methyltrityl side chain. ②The Ⓖ (position: 8) is propargylglycine. ③Ⓚ (2) and Ⓖ (8) are cross-linked by hydrocarbon stapling by 1,3-diploar azide-alkyne cyclization.
    • Stereochemistry

    • L
    • Secondary Structure

    • No structural preference in aqueous solution.
    • Structure Description

    • By CD, we observed that C-MPI-2 and MPI did not display any structural preferences in aqueous solution, whereas C-MPI-1 adopoted a slight α-helical structure.
    • Helical Wheel Diagram

    • DRAMP21503 helical wheel diagram
    • Predicted Structure

    • There is no predicted structure for DRAMP21503.
    • Formula

    • C₈₁H₁₃₈N₂₂O₁₆
    • Absent Amino Acids

    • CDEFGHMNPRSTVY
    • Common Amino Acids

    • KL
    • Mass

    • 1676.13
    • PI

    • /
    • Basic Residues

    • 3
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 8
    • Hydrophobicity

    • /
    • Polar Residues

    • 0

DRAMP21503

  • Literature 1
    • Title

    • Intramolecular cyclization of the antimicrobial peptide Polybia-MPI with triazole stapling: influence on stability and bioactivity
    • Reference

    • J Pept Sci. 2017 Nov;23(11):824-832. doi: 10.1002/psc.3031. Epub 2017 Aug 23.
    • Author

    • Beijun Liu, Wei Zhang, Sanhu Gou, Haifeng Huang, Jia Yao, Zhibin Yang, Hui Liu, Chao Zhong, Beiyin Liu, Jingman Ni, Rui Wang