General Information

    • DRAMP ID

    • DRAMP18443

    • Peptide Name

    • Smp24 (scorpions, arachnids, Chelicerata, arthropods, invertebrates, animals)

    • Source

    • venom, Scorpio maurus palmatus

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • IWSFLIKAATKLLPSLFGGGKKDS

    • Sequence Length

    • 24

    • UniProt Entry

    • No entry found

    • Protein Existence

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Antifungal

    • Target Organism

    • Active against B. subtilis NCIMB 8024, S. epidermidis sp., S. aureus SH100 (MIC 4-8 ug/ml), E. coli JM109 (MIC 64 ug/ml), and C. albicans (MIC 32 ug/ml).

    • Hemolytic Activity

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

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Cell membrance

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

    • Helix

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP18443 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP18443.

Physicochemical Information

    • Formula

    • C123H197N29O31

    • Absent Amino Acids

    • CEHMNQRVY

    • Common Amino Acids

    • KL

    • Mass

    • 2578.09

    • PI

    • 10

    • Basic Residues

    • 4

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 11

    • Net Charge

    • +3

    • Boman Index

    • 56

    • Hydrophobicity

    • 0.313

    • Aliphatic Index

    • 105.83

    • Half Life

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

    • Extinction Coefficient Cystines

    • 5500

    • Absorbance 280nm

    • 239.13

    • Polar Residues

    • 7

DRAMP18443

DRAMP18443 chydropathy plot

Comments Information

    • Removal of the N-terminal four residues increases peptide cell selectivity.

Literature Information

  • ·Literature 1

    • Title

    • Characterisation of three alpha-helical antimicrobial peptides from the venom of Scorpio maurus palmatus

    • Reference

    • Toxicon. 2016 Jul;117:30-6.

    • Author

    • Harrison PL, Abdel-Rahman MA, Strong PN, Tawfik MM, Miller K.