Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1
Pathogenesis-related (PR)-10 proteins, due to their particular secondary structure, can bind various ligands which could be important for their biological function. Accordingly, the PR-10 protein Mal d 1, the major apple allergen, probably also binds molecules in the hydrophobic cavity of its second...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-11-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/10/11/2771 |
| _version_ | 1827676600122998784 |
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| author | Soraya Chebib Wilfried Schwab |
| author_facet | Soraya Chebib Wilfried Schwab |
| author_sort | Soraya Chebib |
| collection | DOAJ |
| description | Pathogenesis-related (PR)-10 proteins, due to their particular secondary structure, can bind various ligands which could be important for their biological function. Accordingly, the PR-10 protein Mal d 1, the major apple allergen, probably also binds molecules in the hydrophobic cavity of its secondary structure, but it has not yet been investigated in this respect. In this study, various natural products found in apples such as flavonoids, glutathione (GSH), and glutathione disulfide (GSSG) were investigated as possible ligands of Mal d 1 using microscale thermophoresis. Dissociation constants of 16.39 µM, 29.51 µM, 35.79 µM, and 0.157 µM were determined for catechin, quercetin-3-<i>O</i>-rhamnoside, GSH, and GSSG, respectively. Molecular docking was performed to better understand the underlying binding mechanism and revealed hydrophobic interactions that stabilize the ligands within the pocket while hydrophilic interactions determine the binding of both GSH derivatives. The binding of these ligands could be important for the allergenicity of the PR-10 protein and provide further insights into its physiological role. |
| first_indexed | 2024-03-10T05:29:41Z |
| format | Article |
| id | doaj.art-93baeccd1f9047dea208a428e4a3247b |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-10T05:29:41Z |
| publishDate | 2021-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-93baeccd1f9047dea208a428e4a3247b2023-11-22T23:21:47ZengMDPI AGFoods2304-81582021-11-011011277110.3390/foods10112771Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1Soraya Chebib0Wilfried Schwab1Biotechnology of Natural Products, Technical University Munich, Liesel-Beckmann-Str. 1, 85354 Freising, GermanyBiotechnology of Natural Products, Technical University Munich, Liesel-Beckmann-Str. 1, 85354 Freising, GermanyPathogenesis-related (PR)-10 proteins, due to their particular secondary structure, can bind various ligands which could be important for their biological function. Accordingly, the PR-10 protein Mal d 1, the major apple allergen, probably also binds molecules in the hydrophobic cavity of its secondary structure, but it has not yet been investigated in this respect. In this study, various natural products found in apples such as flavonoids, glutathione (GSH), and glutathione disulfide (GSSG) were investigated as possible ligands of Mal d 1 using microscale thermophoresis. Dissociation constants of 16.39 µM, 29.51 µM, 35.79 µM, and 0.157 µM were determined for catechin, quercetin-3-<i>O</i>-rhamnoside, GSH, and GSSG, respectively. Molecular docking was performed to better understand the underlying binding mechanism and revealed hydrophobic interactions that stabilize the ligands within the pocket while hydrophilic interactions determine the binding of both GSH derivatives. The binding of these ligands could be important for the allergenicity of the PR-10 protein and provide further insights into its physiological role.https://www.mdpi.com/2304-8158/10/11/2771Mal d 1ligandglutathione |
| spellingShingle | Soraya Chebib Wilfried Schwab Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1 Foods Mal d 1 ligand glutathione |
| title | Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1 |
| title_full | Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1 |
| title_fullStr | Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1 |
| title_full_unstemmed | Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1 |
| title_short | Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1 |
| title_sort | microscale thermophoresis reveals oxidized glutathione as high affinity ligand of mal d 1 |
| topic | Mal d 1 ligand glutathione |
| url | https://www.mdpi.com/2304-8158/10/11/2771 |
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