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The Extracellular Domain of Human High Affinity Copper Transporter (hNdCTR1), Synthesized by E. coli Cells, Chelates Silver and Copper Ions In Vivo

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Department of Biophysics, Peter the Great St. Petersburg Polytechnic University, Politekhnicheskaya str., 29, St.-Petersburg 195251, Russia
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Department of Modern Functional Materials, ITMO University, Kronverksky av., 49, St.-Petersburg 197101, Russia
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Center of Nanoheterostructures Physics, Ioffe Institute, Politekhnicheskaya str., 26, St.-Petersburg 194021, Russia
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Department of Zoology, Herzen State Pedagogical University of Russia, Kazanskaya str., 6, St.-Petersburg 191186, Russia
*
Author to whom correspondence should be addressed.
Academic Editor: Eugene Permyakov
Biomolecules 2017, 7(4), 78; https://doi.org/10.3390/biom7040078
Received: 9 August 2017 / Revised: 22 October 2017 / Accepted: 27 October 2017 / Published: 3 November 2017
There is much interest in effective copper chelators to correct copper dyshomeostasis in neurodegenerative and oncological diseases. In this study, a recombinant fusion protein for expression in Escherichia coli cells was constructed from glutathione-S-transferase (GST) and the N-terminal domain (ectodomain) of human high affinity copper transporter CTR1 (hNdCTR1), which has three metal-bound motifs. Several biological properties of the GST-hNdCTR1 fusion protein were assessed. It was demonstrated that in cells, the protein was prone to oligomerization, formed inclusion bodies and displayed no toxicity. Treatment of E. coli cells with copper and silver ions reduced cell viability in a dose- and time-dependent manner. Cells expressing GST-hNdCTR1 protein demonstrated resistance to the metal treatments. These cells accumulated silver ions and formed nanoparticles that contained AgCl and metallic silver. In this bacterial population, filamentous bacteria with a length of about 10 µm were often observed. The possibility for the fusion protein carrying extracellular metal binding motifs to integrate into the cell’s copper metabolism and its chelating properties are discussed. View Full-Text
Keywords: copper transporter 1 metal-binding extracellular domain cloning; copper/silver chelation; Escherichia coli filamentous growth; secondary silver nanoparticles formation copper transporter 1 metal-binding extracellular domain cloning; copper/silver chelation; Escherichia coli filamentous growth; secondary silver nanoparticles formation
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Sankova, T.P.; Orlov, I.A.; Saveliev, A.N.; Kirilenko, D.A.; Babich, P.S.; Brunkov, P.N.; Puchkova, L.V. The Extracellular Domain of Human High Affinity Copper Transporter (hNdCTR1), Synthesized by E. coli Cells, Chelates Silver and Copper Ions In Vivo. Biomolecules 2017, 7, 78.

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