General Information

    • DRAMP ID

    • DRAMP03222

    • Peptide Name

    • M-ctenitoxin-Cs1a (M-CNTX-Cs1a; Cupiennin-1a; spiders, Arthropods, animals)

    • Source

    • Cupiennius salei (Wandering spider)

    • Family

    • Belongs to the cupiennin family

    • Gene

    • Not found

    • Sequence

    • GFGALFKFLAKKVAKTVAKQAAKQGAKYVVNKQME

    • Sequence Length

    • 35

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Insecticidal

    • Target Organism

      • [Ref.11792701]Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=0.31-0.63 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=0.31-0.63 µM);
      • Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=0.31-0.63 µM), Enterococcus faecalis ATCC 29212 (MIC=2.50-5.00 µM).

    • Hemolytic Activity

      • [Ref.11792701]EC50=24.4 μM against human red blood cells.

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • calcium calmodulin

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Nonterminal Modifications and Unusual Amino Acids

    • Free

    • Stereochemistry

    • L

    • Structure

    • Alpha helix (3 helices; 11 residues)

    • Structure Description

    • The peptide adopts a helix-hinge-helix structure in a membrane mimicking solvent. The hinge may play a role in allowing the amphipathic N-terminal helix and polar C-terminal helix to orient independently upon membrane binding, in order to achieve maximal antibacterial efficacy.(Ref.2)

    • Helical Wheel Diagram

    • DRAMP03222 helical wheel diagram

    • PDB ID

    • 2K38 resolved by NMR.

    • Predicted Structure

    • There is no predicted structure for DRAMP03222.

Physicochemical Information

    • Formula

    • C176H289N47O44S

    • Absent Amino Acids

    • CDHIPRSW

    • Common Amino Acids

    • K

    • Mass

    • 3799.58

    • PI

    • 10.3

    • Basic Residues

    • 8

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 16

    • Net Charge

    • +7

    • Boman Index

    • -24.4

    • Hydrophobicity

    • -0.131

    • Aliphatic Index

    • 75.43

    • Half Life

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

    • Extinction Coefficient Cystines

    • 1490

    • Absorbance 280nm

    • 43.82

    • Polar Residues

    • 6

DRAMP03222

DRAMP03222 chydropathy plot

Comments Information

    • Function

    • Has antimicrobial activity. Has insecticidal and hemolytic activities. Probably acts by disturbing membrane Function

Literature Information

  • ·Literature 1

    • Title

    • Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae).

    • Reference

    • J Biol Chem. 2002 Mar 29;277(13):11208-11216.

    • Author

    • Kuhn-Nentwig L, Muller J, Schaller J, Walz A, Dathe M, Nentwig W.
  • ·Literature 2

    • Title

    • Solution structure and interaction of cupiennin 1a, a spider venom peptide, with phospholipid bilayers.

    • Reference

    • Biochemistry. 2007 Mar 20;46(11):3576-3585.

    • Author

    • Pukala TL, Boland MP, Gehman JD, Kuhn-Nentwig L, Separovic F, Bowie JH.