• • 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

• • UniProt Entry

  • P84568

• • Protein Existence

  • Protein level

• • 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

• • 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

  • 

• • PDB ID

  • 2JQ1 resolved by NMR.
• 2JQ1-> 

• Predicted Structure

• Please click DRAMP01303_predicted_structure.pdb to download.

DRAMP01303

• • Function

  • Has antimicrobial activity (By similarity).

• • Tissue specificity

  • Expressed by the skin glands.

• • PTM

  • C-terminal amidation.

• ·Literature 1

• • Title

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

• • Pubmed ID

  • 15752569

• • 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.

• • Pubmed ID

  • 18656510

• • 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.