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Hydrogen-Bonding Interactions in T-2 Toxin Studied Using Solution and Solid-State NMR

The structure of T-2 toxin in the solid-state is limited to X-ray crystallographic studies, which lack sufficient resolution to provide direct evidence for hydrogen-bonding interactions. Furthermore, its solution-structure, despite extensive Nuclear Magnetic Resonance (NMR) studies, has provided lit...

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Autores principales: Chaudhary, Praveen, Shank, Roxanne A., Montina, Tony, Goettel, James T., Foroud, Nora A., Hazendonk, Paul, Eudes, François
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3210463/
https://www.ncbi.nlm.nih.gov/pubmed/22069698
http://dx.doi.org/10.3390/toxins3101310
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author Chaudhary, Praveen
Shank, Roxanne A.
Montina, Tony
Goettel, James T.
Foroud, Nora A.
Hazendonk, Paul
Eudes, François
author_facet Chaudhary, Praveen
Shank, Roxanne A.
Montina, Tony
Goettel, James T.
Foroud, Nora A.
Hazendonk, Paul
Eudes, François
author_sort Chaudhary, Praveen
collection PubMed
description The structure of T-2 toxin in the solid-state is limited to X-ray crystallographic studies, which lack sufficient resolution to provide direct evidence for hydrogen-bonding interactions. Furthermore, its solution-structure, despite extensive Nuclear Magnetic Resonance (NMR) studies, has provided little insight into its hydrogen-bonding behavior, thus far. Hydrogen-bonding interactions are often an important part of biological activity. In order to study these interactions, the structure of T-2 toxin was compared in both the solution- and solid-state using NMR Spectroscopy. It was determined that the solution- and solid-state structure differ dramatically, as indicated by differences in their carbon chemical shifts, these observations are further supported by solution proton spectral parameters and exchange behavior. The slow chemical exchange process and cross-relaxation dynamics with water observed between the hydroxyl hydrogen on C-3 and water supports the existence of a preferential hydrogen bonding interaction on the opposite side of the molecule from the epoxide ring, which is known to be essential for trichothecene toxicity. This result implies that these hydrogen-bonding interactions could play an important role in the biological function of T-2 toxin and posits towards a possible interaction for the trichothecene class of toxins and the ribosome. These findings clearly illustrate the importance of utilizing solid-state NMR for the study of biological compounds, and suggest that a more detailed study of this whole class of toxins, namely trichothecenes, should be pursued using this methodology.
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spelling pubmed-32104632011-11-08 Hydrogen-Bonding Interactions in T-2 Toxin Studied Using Solution and Solid-State NMR Chaudhary, Praveen Shank, Roxanne A. Montina, Tony Goettel, James T. Foroud, Nora A. Hazendonk, Paul Eudes, François Toxins (Basel) Article The structure of T-2 toxin in the solid-state is limited to X-ray crystallographic studies, which lack sufficient resolution to provide direct evidence for hydrogen-bonding interactions. Furthermore, its solution-structure, despite extensive Nuclear Magnetic Resonance (NMR) studies, has provided little insight into its hydrogen-bonding behavior, thus far. Hydrogen-bonding interactions are often an important part of biological activity. In order to study these interactions, the structure of T-2 toxin was compared in both the solution- and solid-state using NMR Spectroscopy. It was determined that the solution- and solid-state structure differ dramatically, as indicated by differences in their carbon chemical shifts, these observations are further supported by solution proton spectral parameters and exchange behavior. The slow chemical exchange process and cross-relaxation dynamics with water observed between the hydroxyl hydrogen on C-3 and water supports the existence of a preferential hydrogen bonding interaction on the opposite side of the molecule from the epoxide ring, which is known to be essential for trichothecene toxicity. This result implies that these hydrogen-bonding interactions could play an important role in the biological function of T-2 toxin and posits towards a possible interaction for the trichothecene class of toxins and the ribosome. These findings clearly illustrate the importance of utilizing solid-state NMR for the study of biological compounds, and suggest that a more detailed study of this whole class of toxins, namely trichothecenes, should be pursued using this methodology. MDPI 2011-10-21 /pmc/articles/PMC3210463/ /pubmed/22069698 http://dx.doi.org/10.3390/toxins3101310 Text en © 2011 by the authors; licensee MDPI, Basel, Switzerland http://creativecommons.org/licenses/by/3.0/ This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Chaudhary, Praveen
Shank, Roxanne A.
Montina, Tony
Goettel, James T.
Foroud, Nora A.
Hazendonk, Paul
Eudes, François
Hydrogen-Bonding Interactions in T-2 Toxin Studied Using Solution and Solid-State NMR
title Hydrogen-Bonding Interactions in T-2 Toxin Studied Using Solution and Solid-State NMR
title_full Hydrogen-Bonding Interactions in T-2 Toxin Studied Using Solution and Solid-State NMR
title_fullStr Hydrogen-Bonding Interactions in T-2 Toxin Studied Using Solution and Solid-State NMR
title_full_unstemmed Hydrogen-Bonding Interactions in T-2 Toxin Studied Using Solution and Solid-State NMR
title_short Hydrogen-Bonding Interactions in T-2 Toxin Studied Using Solution and Solid-State NMR
title_sort hydrogen-bonding interactions in t-2 toxin studied using solution and solid-state nmr
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3210463/
https://www.ncbi.nlm.nih.gov/pubmed/22069698
http://dx.doi.org/10.3390/toxins3101310
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