Copper(II) binding properties of hepcidin

• Main Authors: Kanokwan Kulprachakarn, Yu Lin Chen, Xiaole Kong, Maria C. Arno, Robert C. Hider, Somdet Srichairatanakool, Sukhvinder S. Bansal
• Format: Journal
• Published: 2018
• Subjects: Biochemistry, Genetics and Molecular Biology; Chemistry
• Online Access: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84958772850&origin=inward; http://cmuir.cmu.ac.th/jspui/handle/6653943832/55199
• Institution: Chiang Mai University

© 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.