General Information

    • DRAMP ID

    • DRAMP18137

    • Peptide Name

    • Peptide Hp1239 (Non-disulfide-bridged peptide 5; NDBP-5)

    • Source

    • Heterometrus petersii (Asian forest scorpion)

    • Family

    • Belongs to the scorpion NDBP 5 family

    • Gene

    • Not found

    • Sequence

    • ILSYLWNGIKSIF

    • Sequence Length

    • 13

    • Protein Existence

    • Transcript level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Antiviral

    • Target Organism

    • CC50=26.15 ± 1.91 μM; HC50= 33.32 ± 0.96 μM; EC50=0.41 ± 0.06 μM

    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Not found

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

    • DRAMP18137 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP18137.

Physicochemical Information

    • Formula

    • C348H562N82O103S3

    • Absent Amino Acids

    • CHP

    • Common Amino Acids

    • L

    • Mass

    • 1553.86

    • PI

    • 8.59

    • Basic Residues

    • 6

    • Acidic Residues

    • 10

    • Hydrophobic Residues

    • 29

    • Net Charge

    • -4

    • Boman Index

    • -5052

    • Hydrophobicity

    • 0.36

    • Aliphatic Index

    • 128.06

    • Half Life

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

    • Extinction Coefficient Cystines

    • 6990

    • Absorbance 280nm

    • 105.91

    • Polar Residues

    • 16

DRAMP18137

Comments Information

    • Function

    • Amphipathic peptide with antibacterial activities (By similarity). Shows antiviral activities against the herpes simplex virus type-1. It potently inhibits the initial infection by provoking the rupture of viral envelop and the dissociation of proteins from the virions (EC (50) is 0.41 μM). It also effectively inhibits viral attachment (EC (50) is 5.73 μM), viral entry (EC (50) is 4.32 μM) and viral proliferation after infection (EC (50) is 8.41 μM). Morever, it enters mammalian tested cells (Vero) and reduces the intracellular infectivity.

Literature Information

  • ·Literature 1

    • Title

    • Molecular diversity of toxic components from the scorpionHeterometrus petersii venom revealed by proteomic and transcriptomeanalysiS.

    • Reference

    • Proteomics 10:2471-2485 (2010).

    • Author

    • Ma Y., Zhao Y., Zhao R., Zhang W., He Y., Wu Y., Cao Z., Guo L., Li W.
  • ·Literature 2

    • Title

    • Inhibitory activity and mechanism of two scorpion venom peptidesagainst herpes simplex virus type 1.

    • Reference

    • Antiviral ReS. 102:1-10 (2014).

    • Author

    • Hong W., Li T., Song Y., Zhang R., Zeng Z., Han S. , Zhang X., Wu Y., Li W., Cao Z.