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Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
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Copper(II)-binding equilibria in human blood.

Tiina Kirsipuu1, Anna Zadorožnaja1, Julia Smirnova1

  • 1Department of Chemistry and Biotechnology, Tallinn University of Technology Akadeemia tee 15, 12618, Tallinn, Estonia.

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This study reveals that in human blood, copper (II) primarily binds to ceruloplasmin (CP) and serum albumin (HSA), with alpha-2-macroglobulin (α2M) not binding copper. The research quantifies copper distribution and binding affinities.

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Metallomics

Background:

  • Copper (II) ions are crucial in human blood, primarily binding to serum albumin (HSA), ceruloplasmin (CP), and alpha-2-macroglobulin (α2M).
  • Limited data exists on α2M's copper binding, and the thermodynamics and kinetics of copper distribution remain largely unknown.

Purpose of the Study:

  • To directly determine the Cu(II)-binding affinities of HSA, CP, and α2M using a novel LC-ICP MS approach.
  • To investigate the thermodynamics and kinetics of copper distribution in human blood serum.

Main Methods:

  • Utilized a liquid chromatography-inductively coupled plasma mass spectrometry (LC-ICP MS) technique.
  • Employed competing Cu(II)-binding reference ligands, including histidine (His), to assess binding affinities.
  • Investigated metal release rates and dissociation constants (KD) for various copper complexes.

Main Results:

  • Demonstrated that α2M does not bind Cu(II) ions, contrary to previous inconclusive evidence.
  • Found that ~75% of Cu(II) in human blood serum is non-exchangeably bound to CP.
  • Identified an equilibrium between HSA (~25%) and Cu(II)-His-Xaa ternary complexes (~0.2%) for the remaining exchangeable copper.

Conclusions:

  • Established the primary binding proteins for Cu(II) in human blood serum as CP and HSA.
  • Quantified the distribution of exchangeable and non-exchangeable copper, highlighting the role of HSA and ternary complexes.
  • The study provides crucial thermodynamic and kinetic insights into copper distribution in biological systems.