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Copper(II) binding properties of hepcidin #MMPMID26883683
Kulprachakarn K; Chen YL; Kong X; Arno MC; Hider RC; Srichairatanakool S; Bansal SS
J Biol Inorg Chem 2016[]; 21 (ä): 329-38 PMID26883683show ga
Hepcidin is a peptide hormone that regulates the homeostasis of iron metabolism. The N-terminal domain of hepcidin is conserved amongst a range of species and is capable of binding CuII and NiII through the amino terminal copper?nickel binding motif (ATCUN). It has been suggested that the binding of copper to hepcidin may have biological relevance. In this study we have investigated the binding of CuII with model peptides containing the ATCUN motif, fluorescently labelled hepcidin and hepcidin using MALDI-TOF mass spectrometry. As with albumin, it was found that tetrapeptide models of hepcidin possessed a higher affinity for CuII than that of native hepcidin. The log K1 value of hepcidin for CuII was determined as 7.7. CuII binds to albumin more tightly than hepcidin (log K1 = 12) and in view of the serum concentration difference of albumin and hepcidin, the bulk of kinetically labile CuII present in blood will be bound to albumin. It is estimated that the concentration of CuII-hepcidin will be less than one femtomolar in normal serum and thus the binding of copper to hepcidin is unlikely to play a role in iron homeostasis. As with albumin, small tri and tetra peptides are poor models for the metal binding properties of hepcidin.Electronic supplementary material: The online version of this article (doi:10.1007/s00775-016-1342-2) contains supplementary material, which is available to authorized users.
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J+Biol+Inorg+Chem 2016 ; 21 (ä): 329-38
