General Information

    • DRAMP ID

    • DRAMP29128

    • Peptide Name

    • Mastoparan-C [L1G, A5K]

    • Source

    • Synthetic construct

    • Family

    • Not found

    • Gene

    • N/A

    • Sequence

    • GNLKKLLAVAKKIL

    • Sequence Length

    • 14

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

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

    • Target Organism

      • [Ref.33285267]Gram-positive bacteria:Staphylococcus aureus ATCC 25923(MIC=16 µM); Bacillus subtilis ATCC 23857(MIC=4 µM);
      • Gram-negative bacteria:Escherichia coli ATCC 25922(4.5 mM KCl and 0.004 mM FeCl3,MIC=4 µM); Pseudomonas aeruginosa ATCC 9027(0.004 mM FeCl3,MIC=4 µM); Klebsiella pneumoniae ATCC 700603(MIC=16 µM); Escherichia coli ATCC 25922(150mM NaCl,MIC=16 µM); Escherichia coli ATCC 25922(1mM MgCl2,MIC=8 µM); Pseudomonas aeruginosa ATCC 9027(NaCl/MgCl2=150mM/1mM,MIC=32 µM); Pseudomonas aeruginosa ATCC 9027(4.5mM KCl,MIC=16 µM); Escherichia coli(Rifampin-resistant strain,MIC=4 µM).

    • Hemolytic Activity

      • [Ref.33285267]0% hemolysis against mouse erythrocytes at 256 µM.

    • Cytotoxicity

      • [Ref.33285267]65% Killing against Human embryonic kidney HEK293T cells at 128 µM; Human embryonic kidney HEK293T cells(IC50=128 µM).

    • Binding Target

    • liposomes

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Nonterminal Modifications and Unusual Amino Acids

    • None

    • Stereochemistry

    • L

    • Structure

    • Alpha helix,random coil

    • Structure Description

    • The CD spectra in water adopts a random-coil conformation,22.26% α-helix was determined in50% TFE.

    • Helical Wheel Diagram

    • DRAMP29128 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP29128.

Physicochemical Information

    • Formula

    • C71H133N19O16

    • Absent Amino Acids

    • CDEFHMPQRSTWY

    • Common Amino Acids

    • KL

    • Mass

    • 1508.95

    • PI

    • 10.48

    • Basic Residues

    • 4

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 8

    • Net Charge

    • +4

    • Boman Index

    • 436

    • Hydrophobicity

    • 0.571

    • Aliphatic Index

    • 174.29

    • Half Life

      • Mammalian:30 hour
      • Yeast:>20 hour
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 2

DRAMP29128

Comments Information

    • Function

    • when combined with gentamicin, rifampin, and polymyxin B, it demonstrated synergistic or additive activity against E. coli ATCC 25922 and P. aeruginosa ATCC 9027.

Literature Information

  • ·Literature 1

    • Title

    • Newly designed antimicrobial peptides with potent bioactivity and enhanced cell selectivity prevent and reverse rifampin resistance in Gram-negative bacteria.

    • Reference

    • Eur J Pharm Sci. 2021 Mar 1;158:105665.

    • Author

    • Zhu N, Zhong C, Liu T, Zhu Y, Gou S, Bao H, Yao J, Ni J.