• DRAMP ID

    • DRAMP30318
    • Peptide Name

    • Temporin L[Pro3,DLeu9,DHyp10](TL5)
    • Source

    • Synthetic construct(derived from Temporin-L)
    • Family

    • Coronaviridae, Herpesviridae, Paramyxoviridae
    • Gene

    • Not found
    • Sequence

    • FVPWFSKFlxRIL
    • Sequence Length

    • 13
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Not found
    • Biological Activity

    • Antimicrobial, Antiviral
    • Target Organism

      • [Ref.35216177]HSV-1:
        Target OrganismActivity
        inhibition of HSV-1 replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);-
      • HSV-2:
        Target OrganismActivity
        inhibition of HSV-2 replication in Vero cells(IC50>50.00 μM μM,IC90>50.00 μM);-
      • SARS-CoV-2:
        Target OrganismActivity
        inhibition of replication in Vero cells(IC50>50.00 μM μM,IC90>50.00 μM);-
      • HPIV-3: inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);
      • HCoV-229E: inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM);
      • HCoV-OC43: inhibition of replication in Vero cells(IC50>50.00 μM,IC90>50.00 μM).
    • Hemolytic Activity

      • [Ref.35216177]<20% hemolysis against human erythrocytes at concentrations equal or above 25 μM.
    • Cytotoxicity

      • [Ref.35216177]Vero cells:CC50>100.00 μM
    • Binding Target

    • membrane
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Amidation
    • Nonterminal Modifications and Unusual Amino Acids

    • The 'x' at position 10 is D-hydroxyproline (Hyp).
    • Stereochemistry

    • Mixed(D-Leu9,D-Hyp10)
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP30318 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP30318.
    • Formula

    • C75H102N16O11
    • Absent Amino Acids

    • ACDEGHMNQTY
    • Common Amino Acids

    • F
    • Mass

    • 1664.26
    • PI

    • 11
    • Basic Residues

    • 2
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 7
    • Net Charge

    • +2
    • Boman Index

    • 128
    • Hydrophobicity

    • 0.708
    • Aliphatic Index

    • 82.31
    • Half Life

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

    • 5500
    • Absorbance 280nm

    • 458.33
    • Polar Residues

    • 1

DRAMP30318

    • Mechanism

    • TL peptides may be able to selectively induce pore formation in highly curved membrane structures (below ~250 nm in diameter), resulting in membrane lysis once a critical number of pores is formed, with the consequence of viral infectivity reduction.
  • ·Literature 1
    • Title

    • Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs.
    • Reference

    • Int J Mol Sci. 2022 Feb 13;23(4):2060.
    • Author

    • Zannella C, Chianese A, Palomba L, Marcocci ME, Bellavita R, Merlino F, Grieco P, Folliero V, De Filippis A, Mangoni M, Nencioni L, Franci G, Galdiero M.