General Information

    • DRAMP ID

    • DRAMP20958

    • Peptide Name

    • StigA16

    • Source

    • Synthetic construct

    • Family

    • Derived from scorpion venom peptide

    • Gene

    • Not found

    • Sequence

    • FFKLIPKLVKGLISAFK

    • Sequence Length

    • 17

    • UniProt Entry

    • No entry found

    • Protein Existence

    • Synthetic

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiparasitic, Antiproliferative

    • Target Organism

      • [Ref.29670004] Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=2.34 μM), Staphylococcus epidermidis ATCC 122225 (MIC=9.38 μM), Enterococcus faecalis ATCC 4028 (MIC=1.17 μM);
      • Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=2.34 μM), Enterobacter cloacae ATCC 13047 (MIC=9.38 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=1.17 μM);
      • yeasts: Candida albicans ATCC 90028 (MIC=4.69 μM), Candida krusei ATCC 6258 (MIC=9.38 μM), Candida glabrata ATCC 90030 (MIC=9.38 μM);
      • StigA16 inhibit 100% of the epimastigote forms of Trypanosoma cruzi growth at 2.5 µM;
      • HeLa cell line: IC50=13.01 µM

    • Hemolytic Activity

      • [Ref.29670004] Hemolysis 0% at 1.17 [Ref.29670004] Hemolysis 0% at 1.17 μM, hemolysis 2% at 2.34 μM, hemolysis 10% at 4.69 μM, hemolysis 20% at 9.38 μM, hemolysis 35% at 18.75 μM, hemolysis 37% at 37.50 μM, hemolysis 40% at 75.00 μM against human red blood cells

    • Cytotoxicity

      • [Ref.29670004] The cell viability of HeLa cell lines is 15%, 21%, 16%, 9%, 8%, 10% and 11% at peptide concentrations of 2, 4, 8, 10, 15, 20 and 40 μM.
      • The cell viability of 3T3 cell lines is 69%, 77%, 62%, 47%, 21%, 15% and 15% at peptide concentratio

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Nonterminal Modifications and Unusual Amino Acids

    • None

    • Stereochemistry

    • L

    • Structure

    • Alpha helix

    • Structure Description

    • The peptide adopts helical conformation with some random structure at the N- and C-terminals. In sodium phosphate buffer (PBS) and water they have a predominantly random structure, but in 20 mM sodium dodecyl sulfate (SDS) and 2,2,2-trifluoroethanol (TFE) they have a typical alpha-helix structure.

    • Helical Wheel Diagram

    • DRAMP20958 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP20958.

Physicochemical Information

    • Formula

    • C99H161N21O19

    • Absent Amino Acids

    • CDEHMNQRTWY

    • Common Amino Acids

    • K

    • Mass

    • 1949.5

    • PI

    • 10.48

    • Basic Residues

    • 4

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 10

    • Net Charge

    • +4

    • Boman Index

    • 1473

    • Hydrophobicity

    • 0.965

    • Aliphatic Index

    • 137.65

    • Half Life

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

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 2

DRAMP20958

Comments Information

    • Function

    • Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity against yeasts.Antiparasitic Activity against epimastigote forms of Trypanosoma cruzi. Antiproliferative Activity against HeLa cells.

Literature Information

  • ·Literature 1

    • Title

    • Analogs of the Scorpion Venom Peptide Stigmurin: Structural Assessment, Toxicity, and Increased Antimicrobial Activity.

    • Reference

    • Toxins (Basel). 2018 Apr 18;10(4). pii: E161.

    • Author

    • Parente AMS, Daniele-Silva A, Furtado AA, Melo MA, Lacerda AF, Queiroz M, Moreno C, Santos E, Rocha HAO, Barbosa EG, Carvalho E, Silva-Júnior AA, Silva MS, Fernandes-Pedrosa MF.