General Information

    • DRAMP ID

    • DRAMP21502

    • Peptide Name

    • C-MP1-1

    • Sequence

    • IDWKKLLⓀAAKⒼIL

    • Sequence Length

    • 14

    • Original Sequence

    • IDWKKLLDAAKQIL

    • Source

    • Synthetic construct

Activity Information

    • Biological Activity

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

    • Comments

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

    • Target Organism

      • [Ref.28833783] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 64 μM), Bacillus subtilis ATCC 23857 (MIC = 8 μM);
      • Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 64 μM), Pseudomonas aeruginosa ATCC 27853 (No antimicrobial activity)

    • Hemolytic Activity

      • [Ref.28833783] It has 0%, 0%, 2.1%, 9.5%, 22.7%, 25.4% and 34.7% against human red blood cells at peptide concentrations of 0, 5, 10, 25, 50, 75 and 150 μM.

    • Cytotoxicity

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

Structure Information

    • Linear/Cyclic

    • Cyclic (Stapled)

    • N-terminal Modification

    • Acetylation

    • C-terminal Modification

    • Amidation

    • Special Amino Acid and Stapling Position

    • ①The Ⓚ (position: 8) is lysine with the methyltrityl side chain. ②The Ⓖ (position: 12) is propargylglycine. ③Ⓚ (8) and Ⓖ (12) are cross-linked by hydrocarbon stapling by 1,3-diploar azide-alkyne cyclization.

    • Stereochemistry

    • L

    • Secondary Structure

    • ①Slight α-helical structure in aqueous solution. ②Increased α-helical conformation in 30 mM SDS and 50% TFE compared with MPI

    • Structure Description

    • ①By 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. ②C-MPI-1 also had higher α-helicity than MPI in membrane mimicking environments, including 30 mM sodium dodecyl sulfate (SDS) and 50% trifluoroethyl alcohol (TFE).

    • Helical Wheel Diagram

    • DRAMP21502 helical wheel diagram

    • Predicted Structure

    • There is no predicted structure for DRAMP21502.

Physicochemical Information

    • Formula

    • C₈₀H₁₃₅N₂₁O₁₇

    • Absent Amino Acids

    • CEFGHMNPQRSTVY

    • Common Amino Acids

    • KL

    • Mass

    • 1663.09

    • PI

    • /

    • Basic Residues

    • 3

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 8

    • Hydrophobicity

    • /

    • Polar Residues

    • 0

DRAMP21502

Literature Information

  • 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