• DRAMP ID

    • DRAMP02294
    • Peptide Name

    • Gaegurin-4 (Gaegurin 4; GGN4; Frogs, amphibians, animals)
    • Source

    • Glandirana rugosa (Japanese wrinkled frog) (Rana rugosa)
    • Family

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

    • GGN4
    • Sequence

    • GILDTLKQFAKGVGKDLVKGAAQGVLSTVSCKLAKTC
    • Sequence Length

    • 37
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • [Ref.7999137]Gram-positive bacteria: Micrococcus luteus (MIC=2.5 µg/ml), Staphylococcus epidermidis (MIC=10 µg/ml), Bacillus subtilis (MIC=10 µg/ml);
      • Gram-negative bacteria: Klebsiella pneumoniae (MIC=25 µg/ml), Shigella dysentariae (MIC=25 µg/ml), Pseudomonas putida (MIC=100 µg/ml), Pseudomonas aeruginosa (MIC=100 µg/ml), Eshchericia coli (MIC=75 µg/ml);
      • Fungi: Saccharomyces cerevisiae (MIC=200 µg/ml), Candida albicans (MIC=200 µg/ml), Salmonella typhimurium (MIC=200 µg/ml), Proteus mirabilis (MIC>200 µg/ml), Serratia marcescens (MIC>200 µg/ml).
    • Hemolytic Activity

      • [Ref.7999137] It has 0.50% hemolytic activity at 0.1 μg/ml, 0.74% hemolytic activity at 1 μg/ml, 0.78% hemolytic activity at 10 μg/ml, 1.67% hemolytic activity at 100 μg/ml against human red blood cells
    • Cytotoxicity

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

    • Not found
    • Linear/Cyclic

    • Cyclic
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Cyclization (Cys31 and Cys37)
    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bond between Cys31 and Cys37.
    • Stereochemistry

    • L
    • Structure

    • Alpha helix (3 helices; 22 residues)
    • Structure Description

    • In 100% H2O, Gaegurin 4 contains a nascent turn near its C-terminal Rana box. Under a more hydrophobic condition it forms two amphipathic helices, one long encompassing residues 2-23 and the other consisting of residues 25-34 (Ref.2).
    • Helical Wheel Diagram

    • DRAMP02294 helical wheel diagram
    • PDB ID

    • 2G9L resolved by NMR.
    • Predicted Structure

    • There is no predicted structure for DRAMP02294.
    • Formula

    • C165H287N45O49S2
    • Absent Amino Acids

    • EHMNPRWY
    • Common Amino Acids

    • K
    • Mass

    • 3749.49
    • PI

    • 9.51
    • Basic Residues

    • 6
    • Acidic Residues

    • 2
    • Hydrophobic Residues

    • 15
    • Net Charge

    • +4
    • Boman Index

    • -13.17
    • Hydrophobicity

    • 0.33
    • Aliphatic Index

    • 105.41
    • Half Life

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

    • 125
    • Absorbance 280nm

    • 3.47
    • Polar Residues

    • 12

DRAMP02294

DRAMP02294 chydropathy plot
    • Function

    • Has a broad spectrum of activity against both Gram-positive and Gram-negative bacteria, fungi and protozoa. Has hemolytic activity against rabbit red cells.
    • Tissue specificity

    • Expressed by the skin glands.
    • PTM

    • Contains one disulfide bond 31-37.
  • ·Literature 1
    • Title

    • Antimicrobial peptides from the skin of a Korean frog, Rana rugosa.
    • Reference

    • Biochem Biophys Res Commun. 1994 Nov 30;205(1):948-954.
    • Author

    • Park JM, Jung JE, Lee BJ.
  • ·Literature 2
    • Title

    • Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4.
    • Reference

    • Biochem Biophys Res Commun. 2007 Jan 19;352(3):592-597.
    • Author

    • Chi SW, Kim JS, Kim DH, Lee SH, Park YH, Han KH.
  • ·Literature 3
    • Title

    • Structural organization and expression of the gaegurin 4 gene of Rana rugosa.
    • Reference

    • Biochim Biophys Acta. 2000 Jun 21;1492(1):185-190.
    • Author

    • Kwon SY, Carlson BA, Park JM, Lee BJ.