• DRAMP ID

    • DRAMP20932
    • Peptide Name

    • Hp1404
    • Source

    • Heterometrus petersii
    • Family

    • Melittin
    • Gene

    • Not found
    • Sequence

    • GILGKLWEGVKSIF
    • Sequence Length

    • 14
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram-
    • Target Organism

      • [Ref.29379033] Gram-negative bacteria: Pseudomonas aeruginosa ATCC 27853 (MIC=12.5 μM), Pseudomonas aeruginosa 138 (MIC=12.5 μM), Pseudomonas aeruginosa 431 (MIC=12.5 μM), Pseudomonas aeruginosa 434 (MIC=12.5 μM), Pseudomonas aeruginosa 557 (MIC=6.25 μM), Pseudomonas aeruginosa 559 (MIC=25 μM), Pseudomonas aeruginosa 778 (MIC=12.5 μM), Pseudomonas aeruginosa 1034 (MIC=6.25 μM), Pseudomonas aeruginosa 1162 (MIC=12.5 μM), Pseudomonas aeruginosa 3290 (MIC=12.5 μM), Pseudomonas aeruginosa 3399 (MIC=6.25 μM), Pseudomonas aeruginosa 3543 (MIC=6.25 μM), Pseudomonas aeruginosa 3592 (MIC=6.25 μM), Pseudomonas aeruginosa 3904 (MIC=6.25 μM), Pseudomonas aeruginosa 4007 (MIC=25 μM), Pseudomonas aeruginosa 4319 (MIC=12.5 μM), Pseudomonas aeruginosa 4891 (MIC=6.25 μM), Pseudomonas aeruginosa 5018 (MIC=12.5 μM), Pseudomonas aeruginosa 671973 (MIC=3.13 μM)
    • Hemolytic Activity

      • [Ref.29379033]Hemolysis 2% at 12.5 μM against mouse red blood cell, hemolysis 11% at 25.0 μM against mouse red blood cell, hemolysis 55% at 50.0 μM against mouse red blood cell, hemolysis 92% at 100.0 μM against mouse red blood cell, hemolysis 100% at 200.0 μM against mouse red blood cell
    • Cytotoxicity

      • [Ref.29379033] The cell survial against HaCaT cells is 85%, 26%, 5% and 6% at peptide concentrations of 25, 50, 100 and 200 μM
    • Binding Target

    • Lipopolysaccharide (LPS)-binding
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Amidation
    • Nonterminal Modifications and Unusual Amino Acids

    • None
    • Stereochemistry

    • L
    • Structure

    • Alpha helix
    • Structure Description

    • The peptide adopts an alpha-helical conformation in the membrane-mimicking environments and the presence of PE:PG and PC:CH liposomes, adopts a random coil conformation when mixed with PC:CH:SM liposomes.
    • Helical Wheel Diagram

    • DRAMP20932 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP20932.
    • Formula

    • C75H119N17O18
    • Absent Amino Acids

    • ACDHMNPQRTY
    • Common Amino Acids

    • G
    • Mass

    • 1546.87
    • PI

    • 8.59
    • Basic Residues

    • 2
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 7
    • Net Charge

    • +1
    • Boman Index

    • 1054
    • Hydrophobicity

    • 0.671
    • Aliphatic Index

    • 132.14
    • Half Life

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

    • 5500
    • Absorbance 280nm

    • 423.08
    • Polar Residues

    • 4

DRAMP20932

    • Function

    • Antibacterial activity against Gram-negative bacteria.
  • ·Literature 1
    • Title

    • Mechanisms driving the antibacterial and antibiofilm properties of Hp1404 and its analogue peptides against multidrug-resistant Pseudomonas aeruginosa.
    • Reference

    • Sci Rep. 2018 Jan 29;8(1):1763.
    • Author

    • Kim MK, Kang HK, Ko SJ, Hong MJ, Bang JK, Seo CH, Park Y.