Bright Singh, I S; Rosamma, Philip; Chaithanya, E R; Anil Kumar, P R; Sherine, Sonia Cubelio; Naveen, Sathyan(Springer, May 23, 2013)
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Abstract:
Hepcidin is a family of short cysteine-rich
antimicrobial peptides (AMPs) participating in various
physiological functions with inevitable role in host immune
responses. Present study deals with identification and
characterisation of a novel hepcidin isoform from coral fish
Zanclus cornutus. The 81 amino acid (aa) preprohepcidin
obtained from Z. cornutus consists of a hydrophobic aa rich
22 mer signal peptide, a highly variable proregion of 35 aa
and a bioactive mature peptide with 8 conserved cysteine
residues which contribute to the disulphide back bone. The
mature hepcidin, Zc-hepc1 has a theoretical isoelectric
point of 7.46, a predicted molecular weight of 2.43 kDa
and a net positive charge of ?1. Phylogenetic analysis
grouped Z. cornutus hepcidin with HAMP2 group hepcidins
confirming the divergent evolution of hepcidin-like
peptide in fishes. Zc-hepc1 can attain a b-hairpin-like
structure with two antiparallel b-sheets. This is the first
report of an AMP from the coral fish Z. cornutus.
Description:
Probiotics & Antimicro. Prot. (2013) 5:187–194
DOI 10.1007/s12602-013-9139-x