• DRAMP ID

    • DRAMP03587
    • Peptide Name

    • DCD-1 (chain of Dermcidin; Human, mammals, animals)
    • Source

    • Homo sapiens (Human)
    • Family

    • Not found
    • Gene

    • DCD
    • Sequence

    • SSLLEKGLDGAKKAVGGLGKLGKDAVEDLESVGKGAVHDVKDVLDSV
    • Sequence Length

    • 47
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • Gram-negative bacteria: Escherichia coli, Enterococcus faecalis;
      • Gram-positive bacterium: Staphylococcus aureus.
      • Yeast: Candida albicans.
    • Hemolytic Activity

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

      • Not included yet
    • Binding Target

    • May bind IgG
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Alpha helix
    • Structure Description

    • Structural analysis of dermcidin-1L in 50% TFE using an N15-labeled recombinant peptide reveals a long helix-hinge-helix motif, allowing it to associate with bacterial membranes (Jung et al. 2010 BMB Rep. 43: 362-8).
    • Helical Wheel Diagram

    • DRAMP03587 helical wheel diagram
    • PDB ID

    • 2KSG resolved by NMR. 2YMK resolved by X-ray.
  • 2KSG-> 
    • Predicted Structure

    • There is no predicted structure for DRAMP03587.
    • Formula

    • C204H348N56O70
    • Absent Amino Acids

    • CFIMNPQRTWY
    • Common Amino Acids

    • G
    • Mass

    • 4705.34
    • PI

    • 5.07
    • Basic Residues

    • 8
    • Acidic Residues

    • 9
    • Hydrophobic Residues

    • 18
    • Net Charge

    • -1
    • Boman Index

    • -52.38
    • Hydrophobicity

    • -0.111
    • Aliphatic Index

    • 109.79
    • Half Life

      • Mammalian:1.9 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 12

DRAMP03587

DRAMP03587 chydropathy plot
    • Function

    • DCD-1 displays antimicrobial activity thereby limiting skin infection by potential pathogens in the first few hours after bacterial colonization. Highly effective against E.coli, E.faecalis, S.aureus and C.albicans. Optimal pH and salt concentration resemble the conditions in sweat. Also exhibits proteolytic activity. Survival-promoting peptide promotes survival of neurons and displays phosphatase activity.
    • Catalytic activity

    • Preferential cleavage
    • Cofactor

    • Manganese. Required for survival-promoting peptide.
    • Tissue specificity

    • Specifically and constitutively expressed in eccrine sweat gland cells. Secreted into the sweat at a concentration of 1-10 micrograms/ml.
  • ·Literature 1
    • Title

    • Dermcidin: a novel human antibiotic peptide secreted by sweat glands.
    • Reference

    • Nat Immunol. 2001 Dec;2(12):1133-1137.
    • Author

    • Schittek B, Hipfel R, Sauer B, Bauer J, Kalbacher H, Stevanovic S, Schirle M, Schroeder K, Blin N, Meier F, Rassner G, Garbe C.
  • ·Literature 2
    • Title

    • Identification of dermcidin in human gestational tissue and characterization of its proteolytic activity.
    • Reference

    • Biochem Biophys Res Commun. 2007 Jun 15;357(4):828-833.
    • Author

    • Lee Motoyama JP, Kim-Motoyama H, Kim P, Nakagama H, Miyagawa K, Suzuki K.
  • ·Literature 3
    • Title

    • Analysis of the solution structure of the human antibiotic peptide dermcidin and its interaction with phospholipid vesicles.
    • Reference

    • BMB Rep. 2010 May;43(5):362-368.
    • Author

    • Jung HH, Yang ST, Sim JY, Lee S, Lee JY, Kim HH, Shin SY, Kim JI.