General Information

    • DRAMP ID

    • DRAMP02013

    • Peptide Name

    • Brevinin-1Ta (Frogs, amphibians, animals)

    • Source

    • Rana temporaria (European common frog)

    • Family

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

    • Gene

    • Not found

    • Sequence

    • FITLLLRKFICSITKKC

    • Sequence Length

    • 17

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

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

    • Target Organism

    • [Swiss_Prot Entry P82233]Antibacterial activity against representative Gram-negative and Gram-positive bacteria

    • Hemolytic Activity

      • [Ref.10333736]Non-hemolytic

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Cell membrane

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

    • Not found

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP02013 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP02013.

Physicochemical Information

    • Formula

    • C95H163N23O21S2

    • Absent Amino Acids

    • ADEGHMNPQVWY

    • Common Amino Acids

    • IKL

    • Mass

    • 2027.6

    • PI

    • 9.85

    • Basic Residues

    • 4

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 8

    • Net Charge

    • +4

    • Boman Index

    • -2.07

    • Hydrophobicity

    • 1.006

    • Aliphatic Index

    • 137.65

    • Half Life

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

    • Extinction Coefficient Cystines

    • 125

    • Absorbance 280nm

    • 7.81

    • Polar Residues

    • 5

DRAMP02013

Comments Information

    • Function

    • Antibacterial activity against representative Gram-negative and Gram-positive bacteria

Literature Information

  • ·Literature 1

    • Title

    • Antimicrobial peptides from amphibian skin: what do they tell us?

    • Reference

    • Biopolymers. 1998;47(6):435-450.

    • Author

    • Simmaco M, Mignogna G, Barra D.