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Updated: Jun 18, 2025

Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
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Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores

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EPR spectroscopic characterisation of native CuII-binding sites in human serum albumin

Katrin Ackermann1, Dongmei Wu2, Alan J Stewart2

  • 1EaStCHEM School of Chemistry, Biomedical Sciences Research Complex, and Centre of Magnetic Resonance, University of St Andrews, St Andrews, KY16 9ST, UK.

Dalton Transactions (Cambridge, England : 2003)
|July 29, 2024
PubMed

Human serum albumin (HSA) is the most abundant plasma protein, which functions to transport a large range of ligands within the circulation. These interactions have important implications for human health and disease. The primary binding site for CuII ions on HSA is known to be the so-called amino-terminal CuII and NiII binding (ATCUN) motif. However, the number and identity of secondary binding sites is currently not understood. In this study, we harnessed a suite of contemporary electron paramagnetic resonance (EPR) spectroscopy methods to investigate recombinantly produced constructs of HSA bearing single-histidine knockouts, with the aim to characterise its endogenous CuII ion binding sites.

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