Crystallographic and EPR-based characterisation of Cu ²⁺ -binding to serum albumin: ATCUN coordination and additional sites

Michal Gucwa; K.B. Handing; Vanessa Amanda Bijak; Katrin Ackermann; Aisika Chakraborty; Anastasiya Pautarak; Timothy Redpath; Boyang Lin; Joanna Sławek; Claudia A. Blindauer; Alan J. Stewart; Bela E. Bode; W. Minor

doi:10.1039/d6qi00150e

January 1, 2026Inorganic Chemistry FrontiersOpen Access

Crystallographic and EPR-based characterisation of Cu ²⁺ -binding to serum albumin: ATCUN coordination and additional sites

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Key Points

The aim is to characterise the binding affinity of Cu²⁺ to serum albumin and identify coordination sites.
Employing crystallographic and EPR techniques
Examining Cu²⁺ interactions with serum albumin
Identifying ATCUN coordination and additional binding sites.
Reveals specific binding affinity of Cu²⁺ to serum albumin
Identifies key physiological roles in copper transport
Finds additional coordination sites beyond ATCUN.

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Implication

EPR-based analysis reveals insights into Cu-binding affinity in serum albumin, suggesting roles in copper transport.

Abstract

Copper homeostasis is essential for mammalian physiology. Serum albumin plays an important role in plasma copper transport and buffering, yet its Cu²⁺ binding sites have remained incompletely characterised. Here we...

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Gucwa et al. (2026) studied this question.

synapsesocial.com/papers/69b4b9eb18185d8a39802287 https://doi.org/10.1039/d6qi00150e

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Crystallographic and EPR-based characterisation of Cu ²⁺ -binding to serum albumin: ATCUN coordination and additional sites

Key Points

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Implication

Abstract

Discussion

Cite This Study

Crystallographic and EPR-based characterisation of Cu ²⁺ -binding to serum albumin: ATCUN coordination and additional sites

Key Points

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

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