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...
| Main Authors: | , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2011-10-01
|
| Series: | Toxins |
| Subjects: | |
| Online Access: | http://www.mdpi.com/2072-6651/3/10/1310/ |
| _version_ | 1818035130038484992 |
|---|---|
| author | Paul Hazendonk François Eudes Praveen Chaudhary Nora A. Foroud James T. Goettel Tony Montina Roxanne A. Shank |
| author_facet | Paul Hazendonk François Eudes Praveen Chaudhary Nora A. Foroud James T. Goettel Tony Montina Roxanne A. Shank |
| author_sort | Paul Hazendonk |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-10T06:50:09Z |
| format | Article |
| id | doaj.art-96ff5a5b372b4220b92afe7524a069bc |
| institution | Directory Open Access Journal |
| issn | 2072-6651 |
| language | English |
| last_indexed | 2024-12-10T06:50:09Z |
| publishDate | 2011-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Toxins |
| spelling | doaj.art-96ff5a5b372b4220b92afe7524a069bc2022-12-22T01:58:34ZengMDPI AGToxins2072-66512011-10-013101310133110.3390/toxins3101310Hydrogen-Bonding Interactions in T-2 Toxin Studied Using Solution and Solid-State NMRPaul HazendonkFrançois EudesPraveen ChaudharyNora A. ForoudJames T. GoettelTony MontinaRoxanne A. ShankThe 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.http://www.mdpi.com/2072-6651/3/10/1310/T-2 toxintrichotheceneNMRhydrogen-bondingribosometoxinepoxidewater bridgingdeuterium exchangechemical exchange |
| spellingShingle | Paul Hazendonk François Eudes Praveen Chaudhary Nora A. Foroud James T. Goettel Tony Montina Roxanne A. Shank Hydrogen-Bonding Interactions in T-2 Toxin Studied Using Solution and Solid-State NMR Toxins T-2 toxin trichothecene NMR hydrogen-bonding ribosome toxin epoxide water bridging deuterium exchange chemical exchange |
| 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 | T-2 toxin trichothecene NMR hydrogen-bonding ribosome toxin epoxide water bridging deuterium exchange chemical exchange |
| url | http://www.mdpi.com/2072-6651/3/10/1310/ |
| work_keys_str_mv | AT paulhazendonk hydrogenbondinginteractionsint2toxinstudiedusingsolutionandsolidstatenmr AT francoiseudes hydrogenbondinginteractionsint2toxinstudiedusingsolutionandsolidstatenmr AT praveenchaudhary hydrogenbondinginteractionsint2toxinstudiedusingsolutionandsolidstatenmr AT noraaforoud hydrogenbondinginteractionsint2toxinstudiedusingsolutionandsolidstatenmr AT jamestgoettel hydrogenbondinginteractionsint2toxinstudiedusingsolutionandsolidstatenmr AT tonymontina hydrogenbondinginteractionsint2toxinstudiedusingsolutionandsolidstatenmr AT roxanneashank hydrogenbondinginteractionsint2toxinstudiedusingsolutionandsolidstatenmr |