General Information

    • DRAMP ID

    • DRAMP01361

    • Peptide Name

    • Frenatin-2 (Frogs, amphibians, animals)

    • Source

    • Litoria infrafrenata (Giant tree frog) (White-lipped tree frog)

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • GLLGTLGNLLNGLGL

    • Sequence Length

    • 15

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+

    • Target Organism

      • Gram-positive bacteria: Micrococcus luteus (MIC=50 µg/ml).

    • 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

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Nonterminal Modifications and Unusual Amino Acids

    • Free

    • Stereochemistry

    • L

    • Structure

    • Not found

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP01361 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP01361.

Physicochemical Information

    • Formula

    • C64H113N17O19

    • Absent Amino Acids

    • ACDEFHIKMPQRSVWY

    • Common Amino Acids

    • L

    • Mass

    • 1424.7

    • PI

    • 5.52

    • Basic Residues

    • 0

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 7

    • Net Charge

    • 0

    • Boman Index

    • 23.29

    • Hydrophobicity

    • 1.127

    • Aliphatic Index

    • 182

    • Half Life

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

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 8

DRAMP01361

Comments Information

    • Function

    • Wide spectrum antimicrobial peptide. Considered to interact with the outer lipid layer of the bacterial cell, penetrate the bacterial membrane, form ion channels, and ultimately kill the cell.

    • Tissue specificity

    • Expressed by the skin parotoid and/or rostral glands.

    • PTM

    • C-terminal amidation.

Literature Information

  • ·Literature 1

    • Title

    • The structures of the frenatin peptides from the skin secretion of the giant tree frog Litoria infrafrenata.

    • Reference

    • J Pept Sci. 1996 Mar-Apr;2(2):117-124.

    • Author

    • Raftery MJ, Waugh RJ, Bowie JH, Wallace JC, Tyler MJ.