General Information

    • DRAMP ID

    • DRAMP29075

    • Peptide Name

    • dCATH 18 (modified from dCATH)

    • Source

    • Synthetic construct

    • Family

    • Not found

    • Gene

    • N/A

    • Sequence

    • FWQLVPLAIKIYRAWKRR

    • Sequence Length

    • 18

    • 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: S. aureus KCTC 1621 (MIC = 8 μM), S. epidermidis KCTC 1917 (MIC = 16 μM), B. subtilis KCTC 3068 (MIC = 8 μM);
      • Resistant Gram-positive bacteria: MRSA CCARM 3089 (MIC = 32 μM), MRSA CCARM 3090 (MIC = 16 μM), MRSA CCARM 3095 (MIC = 32 μM), VREF ATCC 51559(MIC = 32 μM);
      • Gram-negative bacteria: E. coli KCTC 1682 (MIC = 16 μM), P. aeruginosa KCTC 1637(MIC = 16 μM), S. typhimurium KCTC 1926 (MIC = 8 μM);
      • Resistant Gram-negative bacteria: MDRPAd CCARM 2095 (MIC = 32 μM), MDRPA CCARM 2109 (MIC = 32 μM);
      • Yeast: C. albicans KCTC 7965 (MIC = 16 μM), C. albicans KCTC 7121 (MIC = 16 μM).

    • Hemolytic Activity

      • [Ref.32698035] HC10 = 1.3 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 18 against human bone marrow SH-SY5Y cells is 102%, 83%, 75%, 52%, 23%, 9%, 7%.

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Nonterminal Modifications and Unusual Amino Acids

    • None

    • Stereochemistry

    • L

    • Structure

    • Unknown

    • Structure Description

    • Initially, four analog peptides were designed by truncating two, four, six, and eight amino acids at the N-terminal ends of dCATH peptide. dCATH and its truncated analogs could not adopt the amphipathic α-helical structure since the hydrophobic and charged residues were dispersed all around the molecule.

    • Helical Wheel Diagram

    • DRAMP29075 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP29075.

Physicochemical Information

    • Formula

    • C115H178N32O21

    • Absent Amino Acids

    • CDEGHMNST

    • Common Amino Acids

    • R

    • Mass

    • 2344.88

    • PI

    • 11.73

    • Basic Residues

    • 5

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 10

    • Net Charge

    • +5

    • Boman Index

    • -2656

    • Hydrophobicity

    • -0.128

    • Aliphatic Index

    • 113.89

    • Half Life

      • Mammalian:1.1 hour
      • Yeast:3 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 12490

    • Absorbance 280nm

    • 734.71

    • Polar Residues

    • 1

DRAMP29075

DRAMP29075 chydropathy plot

Comments Information

    • Comment

    • The peptide induces potent antimicrobial activity.

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