General Information

    • DRAMP ID

    • DRAMP01303

    • Peptide Name

    • Phylloseptin-3 (PS-3; Frogs, amphibians, animals)

    • Source

    • Phyllomedusa hypochondrialis (Orange-legged leaf frog)

    • Family

    • Not found

    • Gene

    • psn3

    • Sequence

    • FLSLIPHAINAVSALANHG

    • Sequence Length

    • 19

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

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

    • Target Organism

      • [ATCC Strains]: Gram-positive bacteria: S. aureus (MIC=32.9 µM);
      • Gram-negative bacteria: Escherichia coli (MIC=65.6 µM), Klebsiella pneumoniae (MIC=65.6 µM), Pseudomonas aeruginosa (MIC=65.6 µM). NOTE: Initial inoculum of 108 cells/Ml.
      • [Wild Type]: Gram-positive bacteria: S. aureus (MIC=8.2 µM), S. agalactiae (MIC=4.1 µM);
      • Gram-negative bacteria: Pseudomonas aeruginosa (MIC=32.8 µM), A. calcoaceticus (MIC=4.1 µM).
      • Fungi: Candida albicans (MIC=8.2 µM).

    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry

    • Cytotoxicity

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

    • Binding Target

    • Cell membrane

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Nonterminal Modifications and Unusual Amino Acids

    • Free

    • Stereochemistry

    • L

    • Structure

    • Alpha helix (1 helices; 11 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)

    • Helical Wheel Diagram

    • DRAMP01303 helical wheel diagram

    • PDB ID

    • 2JQ1 resolved by NMR.

    • Predicted Structure

    • There is no predicted structure for DRAMP01303.

Physicochemical Information

    • Formula

    • C89H141N25O24

    • Absent Amino Acids

    • CDEKMQRTWY

    • Common Amino Acids

    • A

    • Mass

    • 1945.25

    • PI

    • 6.92

    • Basic Residues

    • 2

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 11

    • Net Charge

    • +2

    • Boman Index

    • 10.4

    • Hydrophobicity

    • 0.926

    • Aliphatic Index

    • 138.95

    • Half Life

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

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 5

DRAMP01303

DRAMP01303 chydropathy plot

Comments Information

    • Function

    • Has antimicrobial activity (By similarity).

    • Tissue specificity

    • Expressed by the skin glands.

    • PTM

    • C-terminal amidation.

Literature Information

  • ·Literature 1

    • Title

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

    • 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.
  • ·Literature 2

    • 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.

    • 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.