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Non-reducible disulfide bond replacement implies that disulfide exchange is not required for hepcidin–ferroportin interaction

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Abstract

Previous studies have led to opposing hypotheses about the requirement of intermolecular disulfide exchange in the binding of the iron regulatory peptide hepcidin to its receptor ferroportin. To clarify this issue, we used the diaminodiacid approach to replace the disulfide bonds in hepcidin with non-reducible thioether bonds. Our results implied that disulfide exchange is not required for the interaction between hepcidin and ferroportin. This theory is further supported by our development of biologically active minihepcidins that do not show activity dependence on cysteine.

Graphical abstract: Non-reducible disulfide bond replacement implies that disulfide exchange is not required for hepcidin–ferroportin interaction

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Publication details

The article was received on 14 Jan 2019, accepted on 07 Feb 2019 and first published on 08 Feb 2019


Article type: Communication
DOI: 10.1039/C9CC00328B
Citation: Chem. Commun., 2019, Advance Article

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    Non-reducible disulfide bond replacement implies that disulfide exchange is not required for hepcidin–ferroportin interaction

    D. Huang, J. Bai, M. Wu, X. Wang, B. Riedl, E. Pook, C. Alt, M. Erny, Y. Li, D. Bierer, J. Shi and G. Fang, Chem. Commun., 2019, Advance Article , DOI: 10.1039/C9CC00328B

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