• • DRAMP ID

  • DRAMP03057

• • Peptide Name

  • Thanatin(insects, arthropods, invertebrates, animals)

• • Source

  • Podisus maculiventris

• • Family

  • Not found

• • Gene

  • Not found

• • Sequence

  • GSKKPVPIIYCNRRTGKCQRM

• • Sequence Length

  • 21

• • UniProt Entry

  • P55788

• • 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

  • 

• • PDB ID

  • 8TFV

• Predicted Structure

• There is no predicted structure for DRAMP03057.

DRAMP03057

• • 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.

• • Pubmed ID

  • 8577744

• • 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.

• • Pubmed ID

  • 9760181

• • 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.