General Information

    • DRAMP ID

    • DRAMP01302

    • Peptide Name

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

    • Source

    • Phyllomedusa hypochondrialis (Orange-legged leaf frog)

    • Family

    • Not found

    • Gene

    • psn2

    • Sequence

    • FLSLIPHAINAVSTLVHHF

    • Sequence Length

    • 19

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

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

    • 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

    • 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; 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

    • DRAMP01302 helical wheel diagram

    • PDB ID

    • 2JPY resolved by NMR.

    • Predicted Structure

    • There is no predicted structure for DRAMP01302.

Physicochemical Information

    • Formula

    • C101H154N26O24

    • Absent Amino Acids

    • CDEGKMQRWY

    • Common Amino Acids

    • HL

    • Mass

    • 2116.49

    • PI

    • 7.02

    • Basic Residues

    • 3

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 11

    • Net Charge

    • +3

    • Boman Index

    • 12.27

    • Hydrophobicity

    • 1.105

    • 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

Comments Information

    • 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 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.