• DRAMP ID

    • DRAMP29087
    • Peptide Name

    • RiLK1
    • Source

    • Synthetic construct
    • Family

    • Not found
    • Gene

    • N/A
    • Sequence

    • VRLIVKVRIWRR
    • Sequence Length

    • 12
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Synthetic form
    • Biological Activity

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

      • [Ref.32971824] Gram-negative bacteria: E.coli (IC50 = 1.20 ± 0.10 μM, MBC = 2.0 μM), S. Typhimurium (IC50 = 1.30 ± 0.14 μM, MBC = 2.5 μM);
      • Gram-positive bacteria: S. aureus (IC50 = 1.98 ± 0.25 μM, MBC = 16.0 μM), L. monocytogenes (IC50 = 0.46 ± 0.01 μM, MBC = 2.0 μM);
      • Fungi: C. albicans ATCC 14053, A. brasiliensis ATCC 9341. Susceptibility testing clearly showed that RiLK1 was very effective, being able to inhibit 100% growth of both fungi at 25 μM concentration (MFC).
    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry
    • Cytotoxicity

      • [Ref.32971824] It was observed that the cell viability was recorded as 98%, 98.7%, and 98.9% at the concentrations of RiLK1 (10, 25, 50 μM)
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Amidation
    • Nonterminal Modifications and Unusual Amino Acids

    • None
    • Stereochemistry

    • L
    • Structure

    • Disordered structure in aqueous solution; β-sheet in the presence of SDS (3 mM)
    • Structure Description

    • Without SDS: 1.2% α-helix, 47.3% β-sheet, 51.5% random; t = 0 h with SDS: 7.4% α-helix, 51.4% β-sheet, 41.3% random; t = 5 min with SDS: 4.4% α-helix, 53.4% β-sheet, 42.2% random; t = 30 min with SDS: 11% α-helix, 48.7% β-sheet, 40.3% random; t = 1 h with SDS: 9.8% α-helix, 51.1% β-sheet, 39.1% random; t = 5 h with SDS: 6.7% α-helix, 54% β-sheet, 39.3% random; t = 6 h with SDS: 8% α-helix, 52% β-sheet, 40.1% random; t = 24 h with SDS: 8.4% α-helix, 53.6% β-sheet, 38% random
    • Helical Wheel Diagram

    • DRAMP29087 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP29087.
    • Formula

    • C74H132N26O13
    • Absent Amino Acids

    • ACDEFGHMNPQSTY
    • Common Amino Acids

    • R
    • Mass

    • 1594.03
    • PI

    • 12.48
    • Basic Residues

    • 5
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 7
    • Net Charge

    • +5
    • Boman Index

    • -3602
    • Hydrophobicity

    • 0.217
    • Aliphatic Index

    • 170
    • Half Life

      • Mammalian:100 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 5500
    • Absorbance 280nm

    • 500
    • Polar Residues

    • 0

DRAMP29087

    • Comment

    • RiLK1 exerted potent killing effects against the clinical isolate (MBC = 1.25 M), two-fold lower than those observed against the strain isolated from food products and those determined with the parental peptide 1018-K6 against ACSSuT strain, thus, suggesting that RiLK1 might have a high potential also in the medical field.
  • ·Literature 1
    • Title

    • A Safe and Multitasking Antimicrobial Decapeptide: The Road from De Novo Design to Structural and Functional Characterization
    • Reference

    • Int J Mol Sci. 2020 Sep 22;21(18):6952. doi: 10.3390/ijms21186952.
    • Author

    • Agrillo B, Proroga YTR, Gogliettino M, Balestrieri M, Tatè R, Nicolais L, Palmieri G