• DRAMP ID

    • DRAMP01320
    • Peptide Name

    • Ranacyclin-B-AL1 (Frogs, amphibians, animals)
    • Source

    • Amolops loloensis (Ranidae frogs)
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • AAFRGCWTKNYSPKPCL
    • Sequence Length

    • 17
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Not found
    • Biological Activity

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

      • Gram-positive bacteria: Staphylococcus aureus (MIC=51 µM), Bacillus subtilis (MIC=26 µM).
    • 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

    • Not found
    • Linear/Cyclic

    • Cyclic
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Free
    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bond between Cys6 and Cys16.
    • Stereochemistry

    • L
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP01320 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP01320.
    • Formula

    • C88H132N24O22S2
    • Absent Amino Acids

    • DEHIMQV
    • Common Amino Acids

    • ACKP
    • Mass

    • 1942.28
    • PI

    • 9.39
    • Basic Residues

    • 3
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 5
    • Net Charge

    • +3
    • Boman Index

    • -21.42
    • Hydrophobicity

    • -0.465
    • Aliphatic Index

    • 34.71
    • Half Life

      • Mammalian:4.4 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 7115
    • Absorbance 280nm

    • 444.69
    • Polar Residues

    • 7

DRAMP01320

    • Function

    • Has antibacterial activity.
  • ·Literature 1
    • Title

    • Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins.
    • Reference

    • Amino Acids. 2012 Jul;43(1):309-316.
    • Author

    • Yan X, Liu H, Yang X, Che Q, Liu R, Yang H, Liu X, You D, Wang A, Li J, Lai R.