General Information

    • DRAMP ID

    • DRAMP02926

    • Peptide Name

    • Tachyplesin I (Tac; TP1; Horseshoe Crab, arachnids, Chelicerata, arthropods, invertebrates, animals)

    • Source

    • Tachypleus tridentatus (Japanese horseshoe crab)

    • Family

    • Belongs to the tachyplesin/polyphemusin family.

    • Gene

    • Not found

    • Sequence

    • KWCFRVCYRGICYRRCR

    • Sequence Length

    • 17

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral, Anti-HIV, Anti-cancer

    • Target Organism

    • No MICs found in DRAMP database

    • Hemolytic Activity

      • [Ref.29870123] 9.6% hemolytic activity at 8 μg/mL and 72.8% hemolytic activity at 512 μg/mL against human red blood cells.

    • Cytotoxicity

      • [Ref.28429216]It possessed a cytotoxic effect on HL-60 cells (acutehuman promyelocytic leukemia cells) , K562 cells(myelogenous leukemia cells) , TSU cells (prostatecancer cells) .

    • Binding Target

    • Cell membrane

Structure Information

    • Linear/Cyclic

    • Cyclic

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation (Arg17)

    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bond between Cys3 and Cys16,Cys7 and Cys12.

    • Stereochemistry

    • L

    • Structure

    • Beta strand

    • Structure Description

    • This stability is due to the rigid structure imposed by the two disulfide linkages. Its amphipathic nature is closely associated with biological activity. A

    • Helical Wheel Diagram

    • DRAMP02926 helical wheel diagram
  • 1WO0-> 
    1WO1-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP02926.

Physicochemical Information

    • Formula

    • C99H154N34O20S4

    • Absent Amino Acids

    • ADEHLMNPQST

    • Common Amino Acids

    • R

    • Mass

    • 2268.77

    • PI

    • 9.93

    • Basic Residues

    • 6

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 4

    • Net Charge

    • +6

    • Boman Index

    • -60.1

    • Hydrophobicity

    • -0.518

    • Aliphatic Index

    • 40

    • Half Life

      • Mammalian:1.3 hour
      • Yeast:3 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 8730

    • Absorbance 280nm

    • 545.63

    • Polar Residues

    • 7

DRAMP02926

Comments Information

    • Function

    • Significantly inhibits the growth of Gram-negative and Gram-positive bacteria, also anti-HIV activity may be due to the inhibition of virual adsorption to cells.

    • PTM

    • Contains two disulfide bonds 3-16; 7-12 and Arginine amide at R17.

Literature Information

  • ·Literature 1

    • Title

    • Solution and Micelle-Bound Structures of Tachyplesin I and its Active Aromatic Linear Derivatives.

    • Reference

    • Biochemistry 2002; 41: 12359.

    • Author

    • Laederach A, Andreotti AH, Fulton, DB.
  • ·Literature 2

    • Title

    • Tachyplesins isolated from hemocytes of Southeast Asian horseshoe crabs (Carcinoscorpius rotundicauda and Tachypleus gigas): identification of a new tachyplesin, tachyplesin III, and a processing intermediate of its precursor.

    • Reference

    • J Biochem. 1990 Aug;108(2):261-266.

    • Author

    • Muta T, Fujimoto T, Nakajima H, Iwanaga S.
  • ·Literature 3

    • Title

    • Characterization of Tachyplesin Peptides and Their Cyclized Analogues to Improve Antimicrobial and Anticancer Properties.

    • Reference

    • Int J Mol Sci. 2019 Aug 26;20(17):4184.

    • Author

    • Vernen F, Harvey PJ, Dias SA, Veiga AS, Huang YH, Craik DJ, Lawrence N, Troeira Henriques S.