EPR spectroscopy shows that the blood carrier protein, human serum albumin, closely interacts with the N-terminal domain of the copper transporter, Ctr1

The Journal of Physical Chemistry. B
Yulia ShenbergerSharon Ruthstein

Abstract

Copper is an essential metal whose localization within the cells must be carefully controlled to avoid copper dependent redox cycling. Although most of the key proteins involved in cellular copper transfer have been identified, fundamental questions regarding the copper transfer mechanism have yet to be resolved. One of the blood carrier proteins believed to be involved in copper transfer to the cell is human serum albumin (HSA). However, direct evidence for close interaction between HSA and the extracellular domain of the copper transporter Ctr1 has not yet been found. By utilizing EPR spectroscopy, we show here that HSA closely interacts with the first 14 amino acids of the Ctr1, even without the presence of copper ions.

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Citations

Jun 28, 2016·Cell Biochemistry and Biophysics·Christopher E Jones, Lawrence J Berliner
Aug 12, 2016·Metallomics : Integrated Biometal Science·Francis AlbaredeToshiyuki Fujii
Jan 18, 2018·Antioxidants & Redox Signaling·Petra HeffeterChristian R Kowol
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May 13, 2020·The Journal of Physical Chemistry. B·Ortal PerkalSharon Ruthstein
Aug 29, 2019·ACS Omega·Gulshan R Walke, Sharon Ruthstein
Nov 20, 2020·Inorganic Chemistry·Ewelina StefaniakKathryn L Haas

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