Copper(II) binding properties of hepcidin
Tetrapeptide
Metalloprotein
DOI:
10.1007/s00775-016-1342-2
Publication Date:
2016-02-16T06:49:13Z
AUTHORS (7)
ABSTRACT
Hepcidin is a peptide hormone that regulates the homeostasis of iron metabolism. The N-terminal domain hepcidin conserved amongst range species and capable binding CuII NiII through amino terminal copper–nickel motif (ATCUN). It has been suggested copper to may have biological relevance. In this study we investigated with model peptides containing ATCUN motif, fluorescently labelled using MALDI-TOF mass spectrometry. As albumin, it was found tetrapeptide models possessed higher affinity for than native hepcidin. log K 1 value determined as 7.7. binds albumin more tightly (log = 12) in view serum concentration difference hepcidin, bulk kinetically labile present blood will be bound albumin. estimated CuII-hepcidin less one femtomolar normal thus unlikely play role homeostasis. small tri tetra are poor metal properties
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