• DRAMP ID

    • DRAMP29362
    • Peptide Name

    • stLRL
    • Sequence

    • LⓧLRLⓧR
    • Sequence Length

    • 7
    • Original Sequence

    • LALRLAR
    • Source

    • Synthetic construct
    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram-
    • Comments

    • Function: Antibacterial activity against Gram-negative bacteria.
    • Target Organism

      • [Ref.37531494]Gram-negativebacteria:E. coli ATCC25922(MIC=16.00 μM), E. coli UB1005(MIC=16.00 μM), E. coli K99(MIC=16.00 μM), E. coli 987P(MIC=8.00 μM), S. typhimurium ATCC14028(MIC=64.00 μM), P. aeruginosa PAO1(MIC=32.00 μM).
    • Hemolytic Activity

      • [Ref.37531494]MHC>256 μM. MHC is the minimum peptide concentration that caused >5% hemolysis of hRBCs.
    • Cytotoxicity

      • [Ref.37531494]<10% cytotoxicity against human embryonic kidney cells (HEK293T) and intestinal porcine enterocyte cells (IPEC-J2) up to 128 μM. 55.18% cell viability against murine macrophage cells (RAW264.7) at 128 μM.
    • Linear/Cyclic

    • Cyclic (Stapled)
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Amidation
    • Special Amino Acid and Stapling Position

    • ①The Ⓧ (position: 2 and 6) in sequence indicates S-(2,4)-pentenyl alanine. ②Ⓧ (2) and Ⓧ (6) 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

    • DRAMP29362 helical wheel diagram
    • Predicted Structure

    • There is no predicted structure for DRAMP29362.
  • Literature 1
    • Title

    • Ultrashort All-Hydrocarbon Stapled α-Helix Amphiphile as a Potent and Stable Antimicrobial Compound. 
    • Reference

    • J Med Chem. 2023 Aug 24;66(16):11414-11427. 
    • Author

    • Shao C, Jian Q, Li B, Zhu Y, Yu W, Li Z, Shan A.