Please use this identifier to cite or link to this item:
Title: Copper(II) binding properties of hepcidin
Authors: Kanokwan Kulprachakarn
Yu Lin Chen
Xiaole Kong
Maria C. Arno
Robert C. Hider
Somdet Srichairatanakool
Sukhvinder S. Bansal
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Jun-2016
Abstract: © 2016, The Author(s). 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 CuIIand NiIIthrough 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 CuIIwith 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 CuIIthan that of native hepcidin. The log K1value of hepcidin for CuIIwas determined as 7.7. CuIIbinds 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 CuIIpresent 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.
ISSN: 14321327
Appears in Collections:CMUL: Journal Articles

Files in This Item:
There are no files associated with this item.

Items in CMUIR are protected by copyright, with all rights reserved, unless otherwise indicated.