General Information

    • DRAMP ID

    • DRAMP01741

    • Peptide Name

    • Temporin-D (Frogs, amphibians, animals)

    • Source

    • Rana temporaria (European common frog)

    • Family

    • Belongs to the frog skin active peptide family (Brevinin subfamily)

    • Gene

    • Not found

    • Sequence

    • LLPIVGNLLNSLL

    • Sequence Length

    • 13

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+

    • Target Organism

      • [Ref.9022710]Gram-positive bacterium: Bacillus megaterium

    • Hemolytic Activity

      • [Ref.10691983]55% hemolysis at 10 μM, 90% hemolysis at 20 μM, 95% hemolysis at 40μM, 100% hemolysis at 60 μM against human red blood cells.

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Not found

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

    • DRAMP01741 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP01741.

Physicochemical Information

    • Formula

    • C65H115N15O17

    • Absent Amino Acids

    • ACDEFHKMQRTWY

    • Common Amino Acids

    • L

    • Mass

    • 1378.72

    • PI

    • 5.52

    • Basic Residues

    • 0

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 8

    • Net Charge

    • 0

    • Boman Index

    • 22.74

    • Hydrophobicity

    • 1.669

    • Aliphatic Index

    • 232.31

    • Half Life

      • Mammalian:5.5 hour
      • Yeast:3 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 4

DRAMP01741

Comments Information

    • Relative to Temporins A, B, and H, temporin D showed the greatest hemolytic activity. Thus, although it lacks antibacterial activity, this peptide may also plays a role in host defense by showing toxicity to eukaryotes) (Eur. J Biochem 2000; 267

    • 1447-1454).

Literature Information

  • ·Literature 1

    • Title

    • Temporins, antimicrobial peptides from the European red frog Rana temporaria.

    • Reference

    • Eur J Biochem. 1996 Dec 15;242(3):788-792.

    • Author

    • Simmaco M, Mignogna G, Canofeni S, Miele R, Mangoni ML, Barra D.
  • ·Literature 2

    • Title

    • Structure-function relationships of temporins, small antimicrobial peptides from amphibian skin.

    • Reference

    • Eur J Biochem. 2000 Mar;267(5):1447-54.

    • Author

    • Mangoni ML, Rinaldi AC, Di Giulio A, Mignogna G, Bozzi A, Barra D, Simmaco M.