Cargando…
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...
Autores principales: | , , , , , , |
---|---|
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 |
_version_ | 1782215736112971776 |
---|---|
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. |
format | Online Article Text |
id | pubmed-3210463 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT chaudharypraveen hydrogenbondinginteractionsint2toxinstudiedusingsolutionandsolidstatenmr AT shankroxannea hydrogenbondinginteractionsint2toxinstudiedusingsolutionandsolidstatenmr AT montinatony hydrogenbondinginteractionsint2toxinstudiedusingsolutionandsolidstatenmr AT goetteljamest hydrogenbondinginteractionsint2toxinstudiedusingsolutionandsolidstatenmr AT foroudnoraa hydrogenbondinginteractionsint2toxinstudiedusingsolutionandsolidstatenmr AT hazendonkpaul hydrogenbondinginteractionsint2toxinstudiedusingsolutionandsolidstatenmr AT eudesfrancois hydrogenbondinginteractionsint2toxinstudiedusingsolutionandsolidstatenmr |