General Information

    • DRAMP ID

    • DRAMP01607

    • Peptide Name

    • Aurein-1.2 (Frogs, amphibians, animals)

    • Source

    • Litoria raniformis (Southern bell frog)

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • GLFDIIKKIAESF

    • Sequence Length

    • 13

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

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

    • Target Organism

      • Gram-positive bacteria: Bacillus cereus (MIC=100 μg/ml), Leuconostoc lactis (MIC=12 μg/ml), Listeria innocua (MIC=100 μg/ml), Micrococcus luteus (MIC=100 μg/ml), Staphylococcus epidermidis (MIC=50 μg/ml), Streptococcus uberis (MIC=50 μg/ml), Staphylococcus aureus (MIC=8 μmol/L);
      • Gram-negative bacteria: Pasteurella multocida (MIC=100 μg/ml), Escherichia coli (MIC=8 μmol/L);
      • Fungi: Candida albicans (MIC=32 μmol/L)

    • Hemolytic Activity

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

    • 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; 10 residues)

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP01607 helical wheel diagram

    • PDB ID

    • 1VM5 resolved by NMR.
  • 1VM5-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP01607.

Physicochemical Information

    • Formula

    • C71H113N15O19

    • Absent Amino Acids

    • CHMNPQRTVWY

    • Common Amino Acids

    • I

    • Mass

    • 1480.77

    • PI

    • 6.07

    • Basic Residues

    • 2

    • Acidic Residues

    • 2

    • Hydrophobic Residues

    • 7

    • Net Charge

    • 0

    • Boman Index

    • -1.64

    • Hydrophobicity

    • 0.669

    • Aliphatic Index

    • 127.69

    • Half Life

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

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 2

DRAMP01607

Comments Information

    • Function

    • Probably acts by disturbing membrane functions with its amphipathic structure. Aurein 1.2 is HIV active (Wang G et al. 2010 Antimicrob. Agents Chemother. (54) 1343-1346). Aurein 1.2 is also the smallest amphibian peptide to show both antibiotic and Anti-cancer activity. The aurein antibiotics show more activity towards Gram-positive than Gram-negative pathogens. Expressed by the skin dorsal glands.

Literature Information

  • ·Literature 1

    • Title

    • The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.

    • Reference

    • Eur J Biochem. 2000 Sep;267(17):5330-5341.

    • Author

    • Rozek T, Wegener KL, Bowie JH, Olver IN, Carver JA, Wallace JC, Tyler MJ.
  • ·Literature 2

    • Title

    • Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a nontoxic bacterial membrane anchor.

    • Reference

    • J Biol Chem. 2005 Feb 18;280(7):5803-5811.

    • Author

    • Wang G, Li Y, Li X.
  • ·Literature 3

    • Title

    • Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.

    • Reference

    • Peptides. 2004 Jun;25(6):1035-1054.

    • Author

    • Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE.