• • DRAMP ID

  • DRAMP01301

• • Peptide Name

  • Phylloseptin-1 (PS-1; Frogs, amphibians, animals)

• • Source

  • Phyllomedusa hypochondrialis (Orange-legged leaf frog)

• • Family

  • Not found

• • Gene

  • psn1

• • Sequence

  • FLSLIPHAINAVSAIAKHN

• • Sequence Length

  • 19

• • UniProt Entry

  • P84566

• • Protein Existence

  • Protein level

• • Biological Activity

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

• • Target Organism

  • • [Ref.15752569]Gram-positive bacteria: Staphylococcus aureus (MIC=7.9 µM), Enterococcus faecalis (MIC=4.0 µM);
    • Gram-negative bacteria: Escherichia coli (MIC=7.9 µM), Psecdomonas aeruginosa (MIC=4 µM), Psecdomonas aeruginosa wt (MIC=3 µM).

• • Hemolytic Activity

  • • [Ref:15752569]0.3% hemolytic activity at 4 μM, 0.57% hemolytic activity at 8 μM, 0.6% hemolytic activity at 16 μM, 0.98% hemolytic activity at 32 μM, 1.98% hemolytic activity at 64 μM against human red blood cells

• • 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; 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)

• • Helical Wheel Diagram

  • 

• • PDB ID

  • 2JQ0 resolved by NMR.

• Predicted Structure

• There is no predicted structure for DRAMP01301.

DRAMP01301

• • Function

  • Atomic force microscopy experiments indicated that the bacteriolytic properties of these peptides might be related to their disruptive action on the cell membrane. PS-1 did not exhibit significant hemolytic activity on human erythrocytes.

• • 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.