Peptide name : Hepcidin

Source/Organism : Human

Linear/Cyclic : Not found

Chirality : L

Peptide length: 20

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Assay type : Cytotoxicity assay

Assay time : 48h

Activity : MIC : 30mM

Cell line : K562

Cancer type : Not found

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 2199.7969 Dalton

Aliphatic index : 0.39

Instability index : 47.77

Hydrophobicity (GRAVY) : 0.795

Isoelectric point : 8.5294

Charge (pH 7) : 2.7661

Aromaticity : 0.05

Molar extinction coefficient (cysteine, cystine): (0, 500)

Hydrophobic/hydrophilic ratio : 2.33333333

hydrophobic moment : 0.0002

Missing amino acid : W,Q,P,E,D,Y,L,N,A,V

Most occurring amino acid : C

Most occurring amino acid frequency : 8

Least occurring amino acid : F

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.1, 0.1, 0.2)

SMILES Notation: CC[C@H](C)[C@H](N)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)NCC(=O)N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)NCC(=O)N[C@@H](CCSC)C(=O)N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)O)[C@@H](C)O)[C@@H](C)CC

1 : Park CH, et al. Hepcidin, a urinary antimicrobial peptide synthesized in the liver. J Biol Chem. 2001; 276:7806-10. doi: 10.1074/jbc.M008922200

Paper title : Hepcidin, a urinary antimicrobial peptide synthesized in the liver.

Doi : https://doi.org/10.1074/jbc.M008922200

Abstract : Cysteine-rich antimicrobial peptides are abundant in animal and plant tissues involved in host defense. In insects, most are synthesized in the fat body, an organ analogous to the liver of vertebrates. From human urine, we characterized a cysteine-rich peptide with three forms differing by amino-terminal truncation, and we named it hepcidin (Hepc) because of its origin in the liver and its antimicrobial properties. Two predominant forms, Hepc20 and Hepc25, contained 20 and 25 amino acid residues with all 8 cysteines connected by intramolecular disulfide bonds. Reverse translation and search of the data bases found homologous liver cDNAs in species from fish to human and a corresponding human genomic sequence on human chromosome 19. The full cDNA by 5' rapid amplification of cDNA ends was 0.4 kilobase pair, in agreement with hepcidin mRNA size on Northern blots. The liver was the predominant site of mRNA expression. The encoded prepropeptide contains 84 amino acids, but only the 20-25-amino acid processed forms were found in urine. Hepcidins exhibited antifungal activity against Candida albicans, Aspergillus fumigatus, and Aspergillus niger and antibacterial activity against Escherichia coli, Staphylococcus aureus, Staphylococcus epidermidis, and group B Streptococcus. Hepcidin may be a vertebrate counterpart of cysteine-rich antimicrobial peptides produced in the fat body of insects.