General Information

    • DRAMP ID

    • DRAMP03565

    • Peptide Name

    • Human hepcidin-25 (Hepc25; one chain of Hepcidin; Human, mammals, animals)

    • Source

    • Homo sapiens (Human)

    • Family

    • Not found

    • Gene

    • HAMP

    • Sequence

    • DTHFPICIFCCGCCHRSKCGMCCKT

    • Sequence Length

    • 25

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

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

    • Target Organism

      • Gram-negative bacterium: Escherichia coli;
      • Gram-positive bacteria: Staphylococcus aureus, S. epidermidis, group B Streptococcus.
      • Fungi: Candida albicans, Aspergillus fumigatus, Aspergillus niger.

    • Hemolytic Activity

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

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • DNA

Structure Information

    • 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

    • Beta strand

    • Structure Description

    • N-terminus is a metal-binding site. disulfide bonds are essential for antibacterial activity by probably binding to DNA.

    • Helical Wheel Diagram

    • DRAMP03565 helical wheel diagram
  • 1M4F-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP03565.

Physicochemical Information

    • Formula

    • C113H178N34O31S9

    • Absent Amino Acids

    • AELNQVWY

    • Common Amino Acids

    • C

    • Mass

    • 2797.41

    • PI

    • 8.22

    • Basic Residues

    • 5

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 4

    • Net Charge

    • +4

    • Boman Index

    • -22.33

    • Hydrophobicity

    • 0.388

    • Aliphatic Index

    • 31.2

    • Half Life

      • Mammalian:1.1 hour
      • Yeast:3 min
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 500

    • Absorbance 280nm

    • 20.83

    • Polar Residues

    • 13

DRAMP03565

DRAMP03565 chydropathy plot

Comments Information

    • PTM

    • Contains four disulfide bonds 7-22; 10-13; 11-19; 14-22.

    • Tissue specificity

    • Highest expression in liver and to a lesser extent in heart and brain. Low levels in lung, tonsils, salivary gland, trachea, prostate gland, adrenal gland and thyroid gland. Secreted into the urine.

    • Function

    • It showed antimicrobial activities in vitro, this peptide might be the long-sought hormone that regulates iron homeostasis in humans. A pathogen will survive if it can figure out a way to steal iron from the host.

Literature Information

  • ·Literature 1

    • Title

    • LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity. ref2) Hepcidin, a rinary antimicrobial peptide synthesized in the liver.

    • Reference

    • FEBS Lett. 2000 Sep 1;480(2-3):147-150.

    • Author

    • Krause A et al Adermann K.
  • ·Literature 2

    • Title

    • Hepcidin, a urinary antimicrobial peptide synthesized in the liver.

    • Reference

    • J Biol Chem. 2001 Mar 16;276(11):7806-7810.

    • Author

    • Park CH, Valore EV, Waring AJ, Ganz T.
  • ·Literature 3

    • Title

    • The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis.

    • Reference

    • J Biol Chem. 2002 Oct 4;277(40):37597-37603.

    • Author

    • Hunter HN, Fulton DB, Ganz T, Vogel HJ.
  • ·Literature 4

    • Title

    • Hepcidin revisited, disulfide connectivity, dynamics, and structure.

    • Reference

    • J Biol Chem. 2009 Sep 4;284(36):24155-24167.

    • Author

    • Jordan JB, Poppe L, Haniu M, Arvedson T, Syed R, Li V, Kohno H, Kim H, Schnier PD, Harvey TS, Miranda LP, Cheetham J, Sasu BJ.