General Information

    • DRAMP ID

    • DRAMP02136

    • Peptide Name

    • Antimicrobial peptide 7 (XT-7; Frogs, amphibians, animals)

    • Source

    • Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • GLLGPLLKIAAKVGSNLL

    • Sequence Length

    • 18

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

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

    • Target Organism

      • Gram-positive bacterium: Staphylococcus aureus (MIC=5 µM);
      • Gram-negative bacterium: Escherichia coli (MIC=5 µM);
      • yeast Candida albicans (MIC=40 µM).
      • Clinical isolates: Staphylococcus aureus 8325 (MIC=6 µM), Staphylococcus aureus (MRSA) (MIC=7 µM), Staphylococcus epidermidis 1420129 (MIC=3 µM), S. saprophyticus 1950556 (MIC=13 µM), Escherichia coli 25922 (MIC=6 µM), Streptococcus group C 1541035 (MIC=3 µM), Shigella sonnei 1840187 (MIC=35 µM), Pseudomonas aeruginosa 0380972 (MIC=60 µM), Enterobacter cloacae 1441323 (MIC=35 µM).

    • Hemolytic Activity

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

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Cell membrane

Structure Information

    • Linear/Cyclic

    • Not included yet

    • N-terminal Modification

    • Not included yet

    • C-terminal Modification

    • Not included yet

    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet

    • Stereochemistry

    • Not included yet

    • Structure

    • Alpha helix

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP02136 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

Physicochemical Information

    • Formula

    • C83H149N21O21

    • Absent Amino Acids

    • CDEFHMQRTWY

    • Common Amino Acids

    • L

    • Mass

    • 1777.22

    • PI

    • 10

    • Basic Residues

    • 2

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 10

    • Net Charge

    • +2

    • Boman Index

    • 23.78

    • Hydrophobicity

    • 1.122

    • Aliphatic Index

    • 178.89

    • Half Life

      • Mammalian:30 hour
      • Yeast:>20 hour
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 5

DRAMP02136

DRAMP02136 chydropathy plot

Comments Information

    • Function

    • Has very strong antibacterial activity against many Gram-negative bacteria and the Gram-positive bacteria S.pneumoniae and Enterococcus sp. There is moderate antimicrobial activity against the Gram-negative bacterium P.aeruginosa and yeast C. albicans and weaker activity against the Streptococcal strains and E.coli. Has hemolytic activity against human red blood cells (HC50=70 µM). Seems to disrupt the membranes by adopting an alpha-helical conformation.

    • Tissue specificity

    • Expressed by the skin glands.

    • PTM

    • Amidation on Leu-18 is required to adopt an alpha-helical conformation in a hydrophobic solvent. The absence of amidation leads to a decrease in cationicity leading to a more than a 10-fold decrease in antimicrobial activities.

Literature Information

  • ·Literature 1

    • Title

    • Antimicrobial peptides isolated from skin secretions of the diploid frog, Xenopus tropicalis (Pipidae).

    • Reference

    • Biochim Biophys Acta. 2001 Nov 26;1550(1):81-89.

    • Author

    • Ali MF, Soto A, Knoop FC, Conlon JM.