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Production and characterization of functional recombinant hybrid heteropolymers of camel hepcidin and human ferritin H and L chains
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Biosensors & Bioelectronics

ISSN: 2155-6210

Open Access

Production and characterization of functional recombinant hybrid heteropolymers of camel hepcidin and human ferritin H and L chains


7th Euro Biosensors and Bioelectronics Conference

July 10-11, 2017 Berlin, Germany

Mohamed Boumaiza

University Federico II Naples, Italy

Posters & Accepted Abstracts: J Biosens Bioelectron

Abstract :

Hepcidin is a liver-synthesized hormone that plays a central role in the regulation of systemic iron homeostasis. To produce a new tool for its functional properties, the cDNA coding for camel hepcidin-25 was cloned at the 5â??end of human FTH sequence into the pASK-IBA43plus vector for expression in Escherichia coli. The recombinant fusion hepcidinâ??ferritin-H subunit was isolated as an insoluble iron-containing protein. Alone it did not refold in a 24-mer ferritin molecule, but it did when renatured together with H- or L-ferritin chains. We obtained stable ferritin shells exposing about four hepcidin peptides per 24-mer shell. The molecules were then reduced and re-oxidized in a controlled manner to allow the formation of the proper hepcidin disulfide bridges. The functionality of the exposed hepcidin was confirmed by its ability to specifically bind the mouse macrophage cell line J774 that express ferroportin and to promote ferroportin degradation. This chimeric protein may be useful for studying the hepcidinâ??ferroportin interaction in cells and also as drug-delivery agent.

Biography :

Email: m.boumaiza@yahoo.fr

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