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Structure and Affinity of Cu(I) Bound to Human Serum Albumin.

Publication ,  Journal Article
Sendzik, M; Pushie, MJ; Stefaniak, E; Haas, KL
Published in: Inorganic chemistry
December 2017

Human serum albumin (HSA) is a major Cu carrier in human blood and in cerebrospinal fluid. A major assumption is that Cu bound to HSA is in the Cu(II) oxidation state; thus, interactions between HSA and Cu(II) have been intensely investigated for over four decades. HSA has been reported previously to support the reduction of Cu(II) to the Cu(I) oxidation state in the presence of the weak reductant, ascorbate; however, the interactions between HSA and Cu(I) have not been explicitly investigated. Here, we characterize both the apparent affinity of HSA for Cu(I) using solution competition experiments and the coordination structure of Cu(I) bound to HSA using X-ray absorption spectroscopy and in silico modeling. We find that HSA binds to Cu(I) at pH 7.4 with an apparent conditional affinity of KCu(I):HSA = 1014.0 using digonal coordination in a structure that is similar to the bis-His coordination modes characterized for amyloid beta (Aβ) and the prion protein. This high affinity and familiar Cu(I) coordination structure suggests that Cu(I) interaction with HSA in human extracellular fluids is unappreciated in the current scientific literature.

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Published In

Inorganic chemistry

DOI

EISSN

1520-510X

ISSN

0020-1669

Publication Date

December 2017

Volume

56

Issue

24

Start / End Page

15057 / 15065

Related Subject Headings

  • X-Ray Absorption Spectroscopy
  • Serum Albumin, Human
  • Protein Conformation
  • Protein Binding
  • Oxidation-Reduction
  • Models, Molecular
  • Inorganic & Nuclear Chemistry
  • Humans
  • Copper
  • Biological Transport
 

Citation

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Sendzik, M., Pushie, M. J., Stefaniak, E., & Haas, K. L. (2017). Structure and Affinity of Cu(I) Bound to Human Serum Albumin. Inorganic Chemistry, 56(24), 15057–15065. https://doi.org/10.1021/acs.inorgchem.7b02397
Sendzik, Madison, M Jake Pushie, Ewelina Stefaniak, and Kathryn L. Haas. “Structure and Affinity of Cu(I) Bound to Human Serum Albumin.Inorganic Chemistry 56, no. 24 (December 2017): 15057–65. https://doi.org/10.1021/acs.inorgchem.7b02397.
Sendzik M, Pushie MJ, Stefaniak E, Haas KL. Structure and Affinity of Cu(I) Bound to Human Serum Albumin. Inorganic chemistry. 2017 Dec;56(24):15057–65.
Sendzik, Madison, et al. “Structure and Affinity of Cu(I) Bound to Human Serum Albumin.Inorganic Chemistry, vol. 56, no. 24, Dec. 2017, pp. 15057–65. Epmc, doi:10.1021/acs.inorgchem.7b02397.
Sendzik M, Pushie MJ, Stefaniak E, Haas KL. Structure and Affinity of Cu(I) Bound to Human Serum Albumin. Inorganic chemistry. 2017 Dec;56(24):15057–15065.
Journal cover image

Published In

Inorganic chemistry

DOI

EISSN

1520-510X

ISSN

0020-1669

Publication Date

December 2017

Volume

56

Issue

24

Start / End Page

15057 / 15065

Related Subject Headings

  • X-Ray Absorption Spectroscopy
  • Serum Albumin, Human
  • Protein Conformation
  • Protein Binding
  • Oxidation-Reduction
  • Models, Molecular
  • Inorganic & Nuclear Chemistry
  • Humans
  • Copper
  • Biological Transport