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Formation of a highly dense tetra-rhenium cluster in a protein crystal and its implications in medical imaging

The fact that a protein crystal can serve as a chemical reaction vessel is intrinsically fascinating. That it can produce an electron-dense tetranuclear rhenium cluster compound from a rhenium tri­carbonyl tri­bromo starting compound adds to the fascination. Such a cluster has been synthesized previ...

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Autores principales: Brink, Alice, Helliwell, John R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6608631/
https://www.ncbi.nlm.nih.gov/pubmed/31316813
http://dx.doi.org/10.1107/S2052252519006651
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author Brink, Alice
Helliwell, John R.
author_facet Brink, Alice
Helliwell, John R.
author_sort Brink, Alice
collection PubMed
description The fact that a protein crystal can serve as a chemical reaction vessel is intrinsically fascinating. That it can produce an electron-dense tetranuclear rhenium cluster compound from a rhenium tri­carbonyl tri­bromo starting compound adds to the fascination. Such a cluster has been synthesized previously in vitro, where it formed under basic conditions. Therefore, its synthesis in a protein crystal grown at pH 4.5 is even more unexpected. The X-ray crystal structures presented here are for the protein hen egg-white lysozyme incubated with a rhenium tri­carbonyl tri­bromo compound for periods of one and two years. These reveal a completed, very well resolved, tetra-rhenium cluster after two years and an intermediate state, where the carbonyl ligands to the rhenium cluster are not yet clearly resolved, after one year. A dense tetranuclear rhenium cluster, and its technetium form, offer enhanced contrast in medical imaging. Stimulated by these crystallography results, the unusual formation of such a species directly in an in vivo situation has been considered. It offers a new option for medical imaging compounds, particularly when considering the application of the pre-formed tetranuclear cluster, suggesting that it may be suitable for medical diagnosis because of its stability, preference of formation and biological compatibility.
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spelling pubmed-66086312019-07-17 Formation of a highly dense tetra-rhenium cluster in a protein crystal and its implications in medical imaging Brink, Alice Helliwell, John R. IUCrJ Research Papers The fact that a protein crystal can serve as a chemical reaction vessel is intrinsically fascinating. That it can produce an electron-dense tetranuclear rhenium cluster compound from a rhenium tri­carbonyl tri­bromo starting compound adds to the fascination. Such a cluster has been synthesized previously in vitro, where it formed under basic conditions. Therefore, its synthesis in a protein crystal grown at pH 4.5 is even more unexpected. The X-ray crystal structures presented here are for the protein hen egg-white lysozyme incubated with a rhenium tri­carbonyl tri­bromo compound for periods of one and two years. These reveal a completed, very well resolved, tetra-rhenium cluster after two years and an intermediate state, where the carbonyl ligands to the rhenium cluster are not yet clearly resolved, after one year. A dense tetranuclear rhenium cluster, and its technetium form, offer enhanced contrast in medical imaging. Stimulated by these crystallography results, the unusual formation of such a species directly in an in vivo situation has been considered. It offers a new option for medical imaging compounds, particularly when considering the application of the pre-formed tetranuclear cluster, suggesting that it may be suitable for medical diagnosis because of its stability, preference of formation and biological compatibility. International Union of Crystallography 2019-06-13 /pmc/articles/PMC6608631/ /pubmed/31316813 http://dx.doi.org/10.1107/S2052252519006651 Text en © Brink & Helliwell 2019 http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/4.0/
spellingShingle Research Papers
Brink, Alice
Helliwell, John R.
Formation of a highly dense tetra-rhenium cluster in a protein crystal and its implications in medical imaging
title Formation of a highly dense tetra-rhenium cluster in a protein crystal and its implications in medical imaging
title_full Formation of a highly dense tetra-rhenium cluster in a protein crystal and its implications in medical imaging
title_fullStr Formation of a highly dense tetra-rhenium cluster in a protein crystal and its implications in medical imaging
title_full_unstemmed Formation of a highly dense tetra-rhenium cluster in a protein crystal and its implications in medical imaging
title_short Formation of a highly dense tetra-rhenium cluster in a protein crystal and its implications in medical imaging
title_sort formation of a highly dense tetra-rhenium cluster in a protein crystal and its implications in medical imaging
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6608631/
https://www.ncbi.nlm.nih.gov/pubmed/31316813
http://dx.doi.org/10.1107/S2052252519006651
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