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Parahydrogen‐Induced Polarization of Amino Acids

Nuclear magnetic resonance (NMR) has become a universal method for biochemical and biomedical studies, including metabolomics, proteomics, and magnetic resonance imaging (MRI). By increasing the signal of selected molecules, the hyperpolarization of nuclear spin has expanded the reach of NMR and MRI...

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Autores principales: Pravdivtsev, Andrey N., Buntkowsky, Gerd, Duckett, Simon B., Koptyug, Igor V., Hövener, Jan‐Bernd
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8596608/
https://www.ncbi.nlm.nih.gov/pubmed/33635601
http://dx.doi.org/10.1002/anie.202100109
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author Pravdivtsev, Andrey N.
Buntkowsky, Gerd
Duckett, Simon B.
Koptyug, Igor V.
Hövener, Jan‐Bernd
author_facet Pravdivtsev, Andrey N.
Buntkowsky, Gerd
Duckett, Simon B.
Koptyug, Igor V.
Hövener, Jan‐Bernd
author_sort Pravdivtsev, Andrey N.
collection PubMed
description Nuclear magnetic resonance (NMR) has become a universal method for biochemical and biomedical studies, including metabolomics, proteomics, and magnetic resonance imaging (MRI). By increasing the signal of selected molecules, the hyperpolarization of nuclear spin has expanded the reach of NMR and MRI even further (e.g. hyperpolarized solid‐state NMR and metabolic imaging in vivo). Parahydrogen (pH(2)) offers a fast and cost‐efficient way to achieve hyperpolarization, and the last decade has seen extensive advances, including the synthesis of new tracers, catalysts, and transfer methods. The portfolio of hyperpolarized molecules now includes amino acids, which are of great interest for many applications. Here, we provide an overview of the current literature and developments in the hyperpolarization of amino acids and peptides.
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spelling pubmed-85966082021-11-22 Parahydrogen‐Induced Polarization of Amino Acids Pravdivtsev, Andrey N. Buntkowsky, Gerd Duckett, Simon B. Koptyug, Igor V. Hövener, Jan‐Bernd Angew Chem Int Ed Engl Minireviews Nuclear magnetic resonance (NMR) has become a universal method for biochemical and biomedical studies, including metabolomics, proteomics, and magnetic resonance imaging (MRI). By increasing the signal of selected molecules, the hyperpolarization of nuclear spin has expanded the reach of NMR and MRI even further (e.g. hyperpolarized solid‐state NMR and metabolic imaging in vivo). Parahydrogen (pH(2)) offers a fast and cost‐efficient way to achieve hyperpolarization, and the last decade has seen extensive advances, including the synthesis of new tracers, catalysts, and transfer methods. The portfolio of hyperpolarized molecules now includes amino acids, which are of great interest for many applications. Here, we provide an overview of the current literature and developments in the hyperpolarization of amino acids and peptides. John Wiley and Sons Inc. 2021-08-13 2021-10-25 /pmc/articles/PMC8596608/ /pubmed/33635601 http://dx.doi.org/10.1002/anie.202100109 Text en © 2021 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Minireviews
Pravdivtsev, Andrey N.
Buntkowsky, Gerd
Duckett, Simon B.
Koptyug, Igor V.
Hövener, Jan‐Bernd
Parahydrogen‐Induced Polarization of Amino Acids
title Parahydrogen‐Induced Polarization of Amino Acids
title_full Parahydrogen‐Induced Polarization of Amino Acids
title_fullStr Parahydrogen‐Induced Polarization of Amino Acids
title_full_unstemmed Parahydrogen‐Induced Polarization of Amino Acids
title_short Parahydrogen‐Induced Polarization of Amino Acids
title_sort parahydrogen‐induced polarization of amino acids
topic Minireviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8596608/
https://www.ncbi.nlm.nih.gov/pubmed/33635601
http://dx.doi.org/10.1002/anie.202100109
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