EPR Spectroscopy Shows that the Blood Carrier Protein, Human Serum Albumin, Closely Interacts with the N-Terminal Domain of the Copper Transporter, Ctr1

Yulia Shenberger, Amit Shimshi, Sharon Ruthstein

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

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. (Figure Presented).

Original languageEnglish
Pages (from-to)4824-4830
Number of pages7
JournalJournal of Physical Chemistry B
Volume119
Issue number14
DOIs
StatePublished - 9 Apr 2015

Bibliographical note

Publisher Copyright:
© 2015 American Chemical Society.

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