General Information

    • DRAMP ID

    • DRAMP18494

    • Peptide Name

    • TP4

    • Source

    • Oreochromis niloticus (Nile tilapia) (Tilapia nilotica)

    • Family

    • Piscidin

    • Gene

    • TP4

    • Sequence

    • FIHHIIGGLFSAGKAIHRLIRRRRR

    • Sequence Length

    • 25

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antibacterial, Antifungal, anticancer, wound healing, Anti-Gram+, Anti-Gram-, Antimicrobial

    • Target Organism

      • [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=8 μg/ml; MBC=16 μg/ml), Methicillin-resistant Staphylococcus aureus (MIC=16 μg/ml; MBC=32 μg/ml);
      • Gram-negative bacterium: Pseudomonas aeruginosa (MIC=64 μg/ml; MBC=128 μg/ml);
      • Fungi: Candida albicans (MIC=128 μg/ml; MBC=128 μg/ml)

    • Hemolytic Activity

      • [Ref.29040295] 2% hemolysis at 0.78 μg/ml, 5% hemolysis at 1.56 μg/ml, 45% hemolysis at 3.13 μg/ml, 85% hemolysis at 6.25 μg/ml, 98% hemolysis at 12.50 μg/ml, 100% hemolysis at 25.00 μg/ml against mouse red blood cell

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • bacterial outer membrane target protein, OprI-binding

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

    • Alpha helix

    • Structure Description

    • 1.0x sarkosyl can drive TP4 into a conformational change from a non-structure to an alpha-helical structure, and that LPS can also drive TP4 to an alpha-helical structure but with high hydrophobicity and low solubility.

    • Helical Wheel Diagram

    • DRAMP18494 helical wheel diagram

    • Predicted Structure

    • There is no predicted structure for DRAMP18494.

Physicochemical Information

    • Formula

    • C135H226N50O27

    • Absent Amino Acids

    • CDEMNPQTVWY

    • Common Amino Acids

    • R

    • Mass

    • 2981.6

    • PI

    • 12.7

    • Basic Residues

    • 10

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 11

    • Net Charge

    • +10

    • Boman Index

    • -6561

    • Hydrophobicity

    • -0.128

    • Aliphatic Index

    • 117.2

    • Half Life

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

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 4

DRAMP18494

DRAMP18494 chydropathy plot

Comments Information

    • Function

    • Antibacterial activity against the Gram-positive and Gram-negative bacteria. Antifungal activity. Has hemolytic activity.

Literature Information

  • ·Literature 1

    • Title

    • Hydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4.

    • Reference

    • PLoS One. 2017 Oct 17;12(10):e0186442.

    • Author

    • Chang TW, Wei SY, Wang SH, Wei HM, Wang YJ, Wang CF, Chen C, Liao YD.