• DRAMP ID

    • DRAMP00298
    • Peptide Name

    • U1-theraphotoxin-Pc1a (U2-TRTX-Pc1a; Psalmopeotoxin-2; PcFK2; Plants)
    • Source

    • Psalmopoeus cambridgei (Trinidad chevron tarantula)
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • RCLPAGKTCVRGPMRVPCCGSCSQNKCT
    • Sequence Length

    • 28
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antiplasmodial, Cytotoxic
    • Target Organism

    • Plasmodium falciparum (IC50=1.15 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
    • 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

    • DRAMP00298 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP00298.
    • Formula

    • C116H203N41O35S7
    • Absent Amino Acids

    • DEFHIWY
    • Common Amino Acids

    • C
    • Mass

    • 2956.56
    • PI

    • 9.22
    • Basic Residues

    • 5
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 4
    • Net Charge

    • +5
    • Boman Index

    • -52.32
    • Hydrophobicity

    • -0.229
    • Aliphatic Index

    • 38.21
    • Half Life

      • Mammalian:1 hour
      • Yeast:2 min
      • E.coli:2 min
    • Extinction Coefficient Cystines

    • 375
    • Absorbance 280nm

    • 13.89
    • Polar Residues

    • 14

DRAMP00298

DRAMP00298 chydropathy plot
    • Function

    • Possess strong antiplasmodial activity against the intra-erythrocyte stage of P.falciparum in vitro. Specifically interacts with infected erythrocytes. Does not lyse erythrocytes, is not cytotoxic to nucleated mammalian cells, and does not inhibit neuromuscular function. Has neither antibacterial nor antifungal activity.
    • Tissue specificity

    • Expressed by the venom gland.
    • Domain

    • The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin By similarity.
    • Miscellaneous

    • Usually endopeptidases cleave the propeptide at the C-terminus of the basic doublet (Arg-37-38-Arg), but here, it seems that the endopeptidase cleaves the precursor within the doublet.
    • PTM

    • Contains three disulfide bonds (By similarity).
  • ·Literature 1
    • Title

    • Isolation and characterization of Psalmopeotoxin I and II: two novel antimalarial peptides from the venom of the tarantula Psalmopoeus cambridgei.
    • Reference

    • FEBS Lett. 2004 Aug 13;572(1-3):109-117.
    • Author

    • Choi SJ, Parent R, Guillaume C, Deregnaucourt C, Delarbre C, Ojcius DM, Montagne JJ, C©l©rier ML, Phelipot A, Amiche M, Molgo J, Camadro JM, Guette C.