General Information

    • DRAMP ID

    • DRAMP29349

    • Peptide Name

    • TP4-3

    • Sequence

    • FIIⓧKKSⓧGLFKKKAGAⓧKKKⓧIKK

    • Sequence Length

    • 25

    • Original Sequence

    • FIHHIIGGLFSAGKAIHRLIRRRRR

    • Source

    • Synthetic construct

Activity Information

    • Biological Activity

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

    • Comments

    • TP4-3 retained its activity against A. baumannii in the presence of 50% human serum(MIC=3.13 μM; MBC=3.13 μM).

    • Target Organism

      • [Ref.36877022]Gram-positive bacteria: Staphylococcus aureus(MIC>25 μM; MBC>25 μM);
      • Gram-negative bacteria:Acinetobacter baumannii(MIC=3.13 μM; MBC=3.13 μM).

    • Hemolytic Activity

      • [Ref.36877022]It shows 15% hemolysis against human red blood cells at the concentration greater than 100 μM.

    • Cytotoxicity

      • [Ref.36877022]TP4-3 showed <10% cell death at 3.13 μM for HaCaT cells, 3.13 μM for HK-2 cells, and 12.5 μM for RAW 264.7 macrophage cells.

Structure Information

    • Linear/Cyclic

    • Cyclic (Stapled)

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Special Amino Acid and Stapling Position

    • ①The Ⓧ (position: 4, 8, 18 and 22) in sequence indicates Fmoc-(R)-2-(4-pentenyl) alanine.②Ⓧ (4) and Ⓧ (8), Ⓧ (18) and Ⓧ (22) are cross-linked by hydrocarbon stapling respectively.

    • Stereochemistry

    • L

    • Secondary Structure

    • No specific results about the strcture presented in the forms of tables, graphs or words

    • Structure Description

    • No other descriptive information about the structure found in the literature

    • Helical Wheel Diagram

    • DRAMP29349 helical wheel diagram

    • Predicted Structure

    • There is no predicted structure for DRAMP29349.

Physicochemical Information

    • Formula

    • C62H93N13O15

    • Absent Amino Acids

    • ACHMNPQRTVWY

    • Common Amino Acids

    • FIKX

    • Mass

    • 2902.78

    • PI

    • 11.11

    • Basic Residues

    • 2

    • Acidic Residues

    • 2

    • Hydrophobic Residues

    • 5

    • Hydrophobicity

    • 18.46

    • Polar Residues

    • 2

DRAMP29349

Literature Information

  • Literature 1

    • Title

    • Rational Design of Stapled Antimicrobial Peptides to Enhance Stability and In Vivo Potency against Polymicrobial Sepsis. 

    • Reference

    • Microbiol Spectr. 2023 Mar 6;11(2):e0385322.

    • Author

    • Yeh JC, Hazam PK, Hsieh CY, Hsu PH, Lin WC, Chen YR, Li CC, Chen JY.