• DRAMP ID

    • DRAMP03724
    • Peptide Name

    • Pandinin-2 (Pin2; Arthropods, animals)
    • Source

    • Pandinus imperator (Emperor scorpion)
    • Family

    • Belongs to the scorpion NDBP 4 family
    • Gene

    • Not found
    • Sequence

    • FWGALAKGALKLIPSLFSSFSKKD
    • Sequence Length

    • 24
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • [Ref.11563967]Gram-negative bacteria: Pseudomonas aeruginosa (MIC=38.2 µM), Escherichia coli (MIC=19.1 µM);#Gram-positive bacteria: Enterococcus faecalis (MIC=2.4 µM), Bacillus subtilis (MIC=4.8 µM), Staphylococcus epidermidis (MIC=4.8 µM), Staphylococcus aureus (MIC=2.4 µM);
      • Yeast: Candida albicans (MIC=19.1 µM).
    • Hemolytic Activity

      • [Ref.11563967]Strong hemolytic activity (11.1-44.5 microM) against sheep erythrocytes
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Cell membrane
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Free
    • Nonterminal Modifications and Unusual Amino Acids

    • Free
    • Stereochemistry

    • L
    • Structure

    • Alpha helix
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP03724 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP03724.
    • Formula

    • C126H195N29O31
    • Absent Amino Acids

    • CEHMNQRTVY
    • Common Amino Acids

    • KLS
    • Mass

    • 2612.11
    • PI

    • 10
    • Basic Residues

    • 4
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 12
    • Net Charge

    • +3
    • Boman Index

    • -1.34
    • Hydrophobicity

    • 0.329
    • Aliphatic Index

    • 93.75
    • Half Life

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

    • 5500
    • Absorbance 280nm

    • 239.13
    • Polar Residues

    • 6

DRAMP03724

DRAMP03724 chydropathy plot
    • Function

    • Disrupts cell membranes through formation of pores. Has strong antimicrobial activity against Gram-positive bacteria and less active against Gram-negative bacteria. Possesses antifungal activity against C. albicans and hemolytic activity against sheep and pig erythrocytes.
    • Tissue specificity

    • Expressed by the venom gland.
  • ·Literature 1
    • Title

    • Characterization of unique amphipathic antimicrobial peptides from venom of the scorpion Pandinus imperator.
    • Reference

    • Biochem J. 2001 Oct 1;359(Pt 1):35-45.
    • Author

    • Corzo G, Escoubas P, Villegas E, Barnham KJ, He W, Norton RS, Nakajima T.
  • ·Literature 2
    • Title

    • Pore formation of phospholipid membranes by the action of two hemolytic arachnid peptides of different size.
    • Reference

    • Biochim Biophys Acta. 2004 Aug 30;1664(2):182-188.
    • Author

    • Belokoneva OS, Satake H, Mal'tseva EL, Pal'mina NP, Villegas E, Nakajima T, Corzo G.
  • ·Literature 3
    • Title

    • Orientation and pore-forming mechanism of a scorpion pore-forming peptide bound to magnetically oriented lipid bilayers.
    • Reference

    • Biophys J. 2004 Oct;87(4):2497-507.
    • Author

    • Nomura K, Corzo G, Nakajima T, Iwashita T.