General Information

    • DRAMP ID

    • DRAMP29083

    • Peptide Name

    • dCATH 12-5 (modified from dCATH 12)

    • Source

    • Synthetic construct

    • Family

    • Not found

    • Gene

    • N/A

    • Sequence

    • LWKKIYRKWKRW

    • Sequence Length

    • 12

    • UniProt Entry

    • No entry found

    • Protein Existence

    • Synthetic form

Activity Information

    • Biological Activity

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

    • Target Organism

      • [Ref.32698035] Gram-positive bacteria:
        Target OrganismActivity
        S. aureus KCTC 1621MIC = 2 μM
        S. epidermidis KCTC 1917MIC = 4 μM
        B. subtilis KCTC 3068 (MIC = 2 μM);-
      • Resistant Gram-positive bacteria:
        Target OrganismActivity
        MRSA CCARM 3089MIC = 16 μM
        MRSA CCARM 3090MIC = 8 μM
        MRSA CCARM 3095MIC = 8 μM
        VREF ATCC 51559(MIC = 8 μM);-
      • Gram-negative bacteria:
        Target OrganismActivity
        E. coli KCTC 1682MIC = 4 μM
        P. aeruginosa KCTC 1637MIC = 2 μM
        S. typhimurium KCTC 1926 (MIC = 2 μM);-
      • Resistant Gram-negative bacteria:
        Target OrganismActivity
        MDRPAd CCARM 2095MIC = 8 μM
        MDRPA CCARM 2109 (MIC = 4 μM);-
      • Yeast: C. albicans KCTC 7965 (MIC = 8 μM), C. albicans KCTC 7121 (MIC = 4 μM).

    • Hemolytic Activity

      • [Ref.32698035] HC10 > 256 μM. Note: HC10 is the peptide concentration that caused 10% hemolysis of sheep red blood cells (sRBCs).

    • Cytotoxicity

      • [Ref.32698035] At the concentration of 1.25, 2.5, 5, 10, 20, 40, 80 μM, the cell survival of dCATH 12-5 against human bone marrow SH-SY5Y cells is 102%, 101%, 100%, 100%, 100%, 95%, 87%.

    • Binding Target

    • Bacterial DNA

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Nonterminal Modifications and Unusual Amino Acids

    • None

    • Stereochemistry

    • L

    • Structure

    • Random coil in buffer; 38.39% α-helix content in 50% TFE; 29.75% α-helix content in 30 mM SDS; 40.40% α-helix content in 0.1% LPS

    • Structure Description

    • Among the 12-meric analog AMPs, Trp rich dCATH 12–4 and dCATH 12-5 displayed high helicity in all membrane-mimetic environment with highest α-helical conformation observed (42.8% and 40.4% respectively) in 0.1% LPS

    • Helical Wheel Diagram

    • DRAMP29083 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP29083.

Physicochemical Information

    • Formula

    • C90H135N25O14

    • Absent Amino Acids

    • ACDEFGHMNPQSTV

    • Common Amino Acids

    • K

    • Mass

    • 1791.22

    • PI

    • 11.22

    • Basic Residues

    • 6

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 5

    • Net Charge

    • +6

    • Boman Index

    • -3535

    • Hydrophobicity

    • -1.692

    • Aliphatic Index

    • 65

    • Half Life

      • Mammalian:5.5 hour
      • Yeast:3 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 17990

    • Absorbance 280nm

    • 1635.45

    • Polar Residues

    • 1

DRAMP29083

Comments Information

    • Comment

    • dCATH 12-5 demonstrated synergistic actions with various conventional antibiotics against antibiotic resistant pathogens, thus indicating their ability as promising adjuncts to combination therapy.

Literature Information

  • ·Literature 1

    • Title

    • Antimicrobial and anti-inflammatory activities of short dodecapeptides derived from duck cathelicidin: Plausible mechanism of bactericidal action and endotoxin neutralization

    • Reference

    • Eur J Med Chem. 2020 Oct 15;204:112580. doi: 10.1016/j.ejmech.2020.112580. Epub 2020 Jul 16.

    • Author

    • Kumar SD, Shin SY