ABSTRACT
Hepcidin is the primary regulatory hormone responsible for lowering the iron content in the blood circulation. Due to its biodegradability and low cytotoxicity, hepcidin is considered as an alternative for iron chelators. The baculovirus expression system may be suitable for human hepcidin production because the expressed proteins generally exhibit proper folding, post-translational modifications, and oligomerization. Using data from two vector maps, pFastBac1 and pFastBac HTB, a unique vector was designed encoding human hepcidin-25 as fusion recombinant peptide. Expression analysis showed that it was expressed as a peptide with a molecular weight near to 5 kDa. After purification and TEV treatment, findings revealed that recombinant human hepcidin-25 was functional and its effect was dose dependent (P=0.001). It was concluded that baculovirus expression was a suitable expression system for production of functional recombinant human hepcidin-25.