• DRAMP ID

    • DRAMP01302
    • Peptide Name

    • Phylloseptin-2 (PS-2; Frogs, amphibians, animals)
    • Source

    • Phyllomedusa hypochondrialis (Orange-legged leaf frog)
    • Family

    • Unknown
    • Gene

    • psn2
    • Sequence

    • FLSLIPHAINAVSTLVHHF
    • Sequence Length

    • 19
    • Evidence code

    • Protein level
    • Biological Activity

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

      • [Ref.18656510][ATCC Strains]: Gram-positive bacteria: S. aureus (MIC=15.1 µM);
      • Gram-negative bacteria: Escherichia coli (MIC=60.4 µM), Klebsiella pneumoniae (MIC=60.4 µM), Pseudomonas aeruginosa (MIC=60.4 µM);
      • [Wild Type]: Gram-positive bacteria: S. aureus (MIC=7.6 µM), S. agalactiae (MIC=1.9 µM);
      • Gram-negative bacteria: Pseudomonas aeruginosa (MIC=60.4 µM), A. calcoaceticus (MIC=3.7 µM);
      • Fungi: Candida albicans (MIC=15.1 µM).
    • Hemolytic activity

      • [Ref:15752569]0.1% hemolytic activity at 4 μM, 0.28% hemolytic activity at 4 μM, 0.7% hemolytic activity at 8 μM, 0.8% hemolytic activity at 16 μM, 1.05% hemolytic activity at 32 μM, 2.05% hemolytic activity at 64 μM against human red blood cells
    • Binding Target

    • Cell membrane
    • Structure

    • Alpha helix (1 helices; 14 residues)
    • Structure Description

    • The antimicrobial phylloseptin peptides adopt alpha-helical conformations in membrane environments which are stabilized by electrostatic interactions of the helix dipole as well as other contributions such hydrophobic and capping interactions.(Ref.2)
    • PDB ID

    • 2JPY resolved by NMR.
    • DRAMP01302 helical wheel diagram
    • 2JPY-> 
    • Formula

    • C101H154N26O24
    • Absent Amino Acids

    • CDEGKMQRWY
    • Common Amino Acids

    • HL
    • Mass

    • 2437.75
    • PI

    • 7.81
    • Basic Residues

    • 3
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 11
    • Boman Index

    • 12.27
    • Hydrophobicity

    • 110.53
    • Aliphatic Index

    • 143.68
    • Half Life

      • Mammalian:1.1 hour
      • Yeast:3 min
      • E.coli:2 min
    • Extinction Coefficient Cystines

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 4

DRAMP01302

DRAMP01302 chydropathy plot
    • Function

    • Has antimicrobial activity. PS-2 did not exhibit significant hemolytic activity on human erythrocytes.
    • Tissue specificity

    • Expressed by the skin glands.
    • PTM

    • C-terminal amidation.
  • Literature 1
    • Reference

    • Peptides. 2006 Sep;27(9):2129-2136.
    • Author

    • Chen T, Zhou M, Gagliardo R, Walker B, Shaw C.
    • Title

    • Elements of the granular gland peptidome and transcriptome persist in air-dried skin of the South American orange-legged leaf frog, Phyllomedusa hypocondrialis.
  • Literature 2
    • Reference

    • Peptides. 2005 Apr;26(4):565-573.
    • Author

    • Leite JR, Silva LP, Rodrigues MI, Prates MV, Brand GD, Lacava BM, Azevedo RB, Bocca AL, Albuquerque S, Bloch C Jr.
    • Title

    • Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides from the Phyllomedusa genus.
  • Literature 3
    • Reference

    • Peptides. 2008 Oct;29(10):1633-1644.
    • Author

    • Resende JM, Moraes CM, Prates MV, Cesar A, Almeida FC, Mundim NC, Valente AP, Bemquerer MP, Piló-Veloso D, Bechinger B.
    • Title

    • Solution NMR structures of the antimicrobial peptides phylloseptin-1, -2, and -3 and biological activity: the role of charges and hydrogen bonding interactions in stabilizing helix conformations.