• DRAMP ID

    • DRAMP03057
    • Peptide Name

    • Thanatin(insects, arthropods, invertebrates, animals)
    • Source

    • Podisus maculiventris
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • GSKKPVPIIYCNRRTGKCQRM
    • Sequence Length

    • 21
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • [Ref.8577744] Gram-positive bacteria: Aerococcus viridans (MIC=0.6-1.2 µM), Micrococcus luteus (MIC=1.2-2.5 µM), Bacillus megaterium (MIC=2.5-5 µM), Bacillus subtilis (MIC=2.5-5 µM), Pediococcus acidilactici (MIC=20-40 µM);
      • Gram-negative bacteria: Escherichia coli D22 (MIC=0.3-0.6 µM), Escherichia coli D31 (MIC=0.3-0.6 µM), Escherichia coli 1106 (MIC=0.6-1.2 µM), Salmonella typhimurium (MIC=0.6-1.2 µM), Klebsiella pneumoniae (MIC=0.6-1.2 µM), Enterobacter cloacae (MIC=1.2-2.5 µM), Erwinia carotovora (MIC=10-20 µM), Pseudomonas aeruginosa (MIC=20-40 µM);
      • Fungi: Neurospora crassa (MIC=0.6-1.2 µM), Botrytis cinerea (MIC=1.2-2.5 µM), Nectria haematococca (MIC=1.2-2.5 µM), Trichoderma viride (MIC=1.2-2.5 µM), Alternaria brassicicola (MIC=2.5-5 µM), Fusarium culmorum (MIC=2.5-5 µM), Ascochyta pisi (MIC=5-10µM), Fusarium oxysporum (MIC=10-20 µM).
    • Hemolytic Activity

      • [Ref.8577744] It exhibits no hemolytic activity at 40 µM against porcine erythrocytes.
    • Cytotoxicity

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

    • Not found
    • Linear/Cyclic

    • Cyclic
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Free
    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bond between Cys11 and Cys18.
    • Stereochemistry

    • L
    • Structure

    • Beta strand
    • Structure Description

    • Contain C-terminally a loop of 6 residues, delineated by an intramolecular disulfide bridge. This loop carries a strong positive charge in both molecules and contains a central threonine residue, which separates two subgroups of electropositivity.
    • Helical Wheel Diagram

    • DRAMP03057 helical wheel diagram
  • 8TFV-> 
    • Predicted Structure

    • There is no predicted structure for DRAMP03057.
    • Formula

    • C103H179N35O27S3
    • Absent Amino Acids

    • ADEFHLW
    • Common Amino Acids

    • KR
    • Mass

    • 2435.95
    • PI

    • 10.47
    • Basic Residues

    • 6
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 3
    • Net Charge

    • +6
    • Boman Index

    • -59.03
    • Hydrophobicity

    • -0.9
    • Aliphatic Index

    • 50.95
    • Half Life

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

    • 1615
    • Absorbance 280nm

    • 80.75
    • Polar Residues

    • 8

DRAMP03057

DRAMP03057 chydropathy plot
    • Function

    • Insect defense peptide with a broad spectrum of activity against Gram-positive and Gram-negative bacteria and fungi. No activity against S.aureus. Stops respiration in bacteria but does not permeabilize their inner membranes. Has no detectable hemolytic activity.
  • ·Literature 1
    • Title

    • Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides.
    • Reference

    • Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1221-1225.
    • Author

    • Fehlbaum P, Bulet P, Chernysh S, Briand JP, Roussel JP, Letellier L, Hetru C, Hoffmann JA.
  • ·Literature 2
    • Title

    • Solution structure of thanatin, a potent bactericidal and fungicidal insect peptide, determined from proton two-dimensional nuclear magnetic resonance data.
    • Reference

    • Eur J Biochem. 1998 Sep 1;256(2):404-410.
    • Author

    • Mandard N, Sodano P, Labbe H, Bonmatin JM, Bulet P, Hetru C, Ptak M, Vovelle F.