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Updated: Mar 25, 2026
Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
Published on: April 5, 2022
Copper(II) binding properties of hepcidin
Kanokwan Kulprachakarn1, Yu-Lin Chen2, Xiaole Kong2
1Faculty of Pharmacy, Payap University, Mae Khao Campus, Chiang Mai, Thailand.
The study found that copper binding to hepcidin is unlikely to impact iron homeostasis. Copper preferentially binds to albumin in blood, making copper-hepcidin complexes negligible in normal serum.
Area of Science:
- Biochemistry
- Metalloprotein Chemistry
Background:
- Hepcidin is a peptide hormone crucial for iron metabolism homeostasis.
- Hepcidin's N-terminal domain features an amino terminal copper-nickel binding motif (ATCUN), capable of binding Cu(II) and Ni(II).
- Previous suggestions posited biological relevance for copper-hepcidin interactions.
Purpose of the Study:
- To investigate the binding affinity of Cu(II) to hepcidin and model peptides.
- To determine the biological significance of copper binding to hepcidin in iron homeostasis.
Main Methods:
- Utilized MALDI-TOF mass spectrometry to analyze Cu(II) binding.
- Employed model peptides with ATCUN motifs and fluorescently labeled hepcidin.
- Quantified binding affinity using log K1 values.
Main Results:
- Tetrapeptide models showed higher Cu(II) affinity than native hepcidin.
- Hepcidin's log K1 for Cu(II) was determined as 7.7.
- Albumin exhibits a stronger affinity (log K1 = 12) for Cu(II) than hepcidin.
Conclusions:
- The bulk of labile Cu(II) in blood is bound by albumin due to concentration differences.
- Cu(II)-hepcidin concentrations are estimated below femtomolar levels in normal serum.
- Copper binding to hepcidin is unlikely to play a significant role in iron homeostasis.
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