• • DRAMP ID

  • DRAMP20895

• • Peptide Name

  • F1A/I2A

• • Source

  • Synthetic construct

• • Family

  • Derived from TP4

• • Gene

  • Not found

• • Sequence

  • AAHHIIGGLFSAGKAIHRLIRRRRR

• • Sequence Length

  • 25

• • UniProt Entry

  • No entry found

• • Protein Existence

  • Synthetic

• • Biological Activity

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

• • Target Organism

  • • [Ref.29040295] Gram-positive bacteria: Staphylococcus aureus (MIC=128 μg/ml; MBC=256 μg/ml);
    • Gram-negative bacteria: Pseudomonas aeruginosa (MIC=256 μg/ml; MBC=256 μg/ml);
    • Fungi: Candida albicans (MIC=64 μg/ml; MBC=128 μg/ml)

• • Hemolytic Activity

  • • [Ref.29040295] 10% haemolysis at 12.50 μg/ml, 15% haemolysis at 25.00 μg/ml, 30% haemolysis at 50.00 μg/ml, 90% haemolysis at 100.00 μg/ml, 95% haemolysis at 200.00 μg/ml, 100% haemolysis at 400.00 μg/ml against mouse red blood cells

• • Cytotoxicity

  • No cytotoxicity information found in the reference(s) presented

• • Binding Target

  • Not found

• • Linear/Cyclic

  • Linear

• • N-terminal Modification

  • Free

• • C-terminal Modification

  • Free

• • Nonterminal Modifications and Unusual Amino Acids

  • None

• • Stereochemistry

  • L

• • Structure

  • Not found

• • Structure Description

  • Not found

• • Helical Wheel Diagram

  • 

• • PDB ID

  • 5H2S

• Predicted Structure

• There is no predicted structure for DRAMP20895.

DRAMP20895

• • Function

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

• ·Literature 1

• • Title

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

• • Pubmed ID

  • 29040295

• • 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.