• DRAMP ID

    • DRAMP29052
    • Peptide Name

    • Brevinin-1GHd
    • Source

    • Sylvirana guentheri (Gunther's frog) (Rana guentheri)
    • Family

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

    • N/A
    • Sequence

    • FLGALFKVASKLVPAAICSISKKC
    • Sequence Length

    • 24
    • Protein Existence

    • Transcript level
    • Biological Activity

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

      • [Ref.32347293] Gram-positive bacteria: S. aureus (MIC = 2 μM/MBC= 4 µM), MRSA(MIC = 4 μM/MBC = 4µM);
      • Gram-negative: E. coli(MIC = 8 μM/MBC = 8 µM), P. aeruginosa(MIC = 32 μM/MBC = 32µM);
      • Fungi: C. albicans(MIC = 4 μM/MBC = 8µM)
    • Hemolytic Activity

      • [Ref.32347293] Brevinin-1GHd displayed 13% hemolysis on horse red blood cells at its highest MIC/MBC value of the tested bacteria P. aeruginosa (32 µM). However, when the concentration increased above 64 μM, the hemolytic activity of Brevinin-1GHd also gradually increased. At the concentration of 64, 128, 256 and 512 μM, it displayed about 36%, 64%, 83% and 108% hemolysis.
    • Cytotoxicity

      • [Ref.32347293]Brevinin-1GHd showed significant cytotoxicity toward human HMEC-1 and HaCaT cells at concentrations of 0.00001 and 0.0001 M, respectively. Brevinin-1GHd induced one cell viability of 56% on HMEC-1 and the other cell viability of 75% on HaCat.
    • Binding Target

    • Cell membrane
    • Linear/Cyclic

    • Cyclic
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Free
    • Nonterminal Modifications and Unusual Amino Acids

    • Free
    • Stereochemistry

    • L
    • Structure

    • α-helical
    • Structure Description

    • The results of CD spectroscopy revealed that Brevinin-1GHd adopt a random coil structure in an aqueous environment, while forming an alpha-helix structure in a membrane-mimetic environment.
    • Helical Wheel Diagram

    • DRAMP29052 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP29052.
    • Formula

    • C116H196N28O28S2
    • Absent Amino Acids

    • DEHMNQRTWY
    • Common Amino Acids

    • AK
    • Mass

    • 2495.12
    • PI

    • 9.7
    • Basic Residues

    • 4
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 13
    • Net Charge

    • +4
    • Boman Index

    • 1698
    • Hydrophobicity

    • 1.108
    • Aliphatic Index

    • 122.08
    • Half Life

      • Mammalian:1.1 hour
      • Yeast:3 min
      • E.coli:2 min
    • Extinction Coefficient Cystines

    • 125
    • Absorbance 280nm

    • 5.43
    • Polar Residues

    • 6

DRAMP29052

DRAMP29052 chydropathy plot
    • Comment

    • Brevinin-1GHd with its excellent antimicrobial and anticancer activities is a promising candidate for a novel antibiotic agent, and study of its structure activity relationships also provided a rational template for further research and peptide analog design. In the reference, the example of Brevinin-1GHd is used to challenge the importance of "Rana-Box", which appears in many AMPs originating from frogs and contains an intermolecular disulfide bridge at the C-terminus of the peptide and seven to nine amino acid residues.
  • ·Literature 1
    • Title

    • Brevinin-1GHd: a novel Hylarana guentheri skin secretion-derived Brevinin-1 type peptide with antimicrobial and anticancer therapeutic potential
    • Reference

    • Biosci Rep. 2020 May 29;40(5):BSR20200019. doi: 10.1042/BSR20200019.
    • Author

    • Jiang Y, Wu Y, Wang T, Chen X, Zhou M, Ma C, Xi X, Zhang Y, Chen T, Shaw C, Wang L.