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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Autores principales:	Soraya Chebib, Wilfried Schwab
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	Mal d 1 ligand glutathione Chemical technology TP1-1185
Acceso en línea:	https://doaj.org/article/93baeccd1f9047dea208a428e4a3247b
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spelling	oai:doaj.org-article:93baeccd1f9047dea208a428e4a3247b2021-11-25T17:35:27ZMicroscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 110.3390/foods101127712304-8158https://doaj.org/article/93baeccd1f9047dea208a428e4a3247b2021-11-01T00:00:00Zhttps://www.mdpi.com/2304-8158/10/11/2771https://doaj.org/toc/2304-8158Pathogenesis-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.Soraya ChebibWilfried SchwabMDPI AGarticleMal d 1ligandglutathioneChemical technologyTP1-1185ENFoods, Vol 10, Iss 2771, p 2771 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Mal d 1 ligand glutathione Chemical technology TP1-1185
spellingShingle	Mal d 1 ligand glutathione Chemical technology TP1-1185 Soraya Chebib Wilfried Schwab Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1
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.
format	article
author	Soraya Chebib Wilfried Schwab
author_facet	Soraya Chebib Wilfried Schwab
author_sort	Soraya Chebib
title	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_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_sort	microscale thermophoresis reveals oxidized glutathione as high-affinity ligand of mal d 1
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/93baeccd1f9047dea208a428e4a3247b
work_keys_str_mv	AT sorayachebib microscalethermophoresisrevealsoxidizedglutathioneashighaffinityligandofmald1 AT wilfriedschwab microscalethermophoresisrevealsoxidizedglutathioneashighaffinityligandofmald1
_version_	1718412179005243392

Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1

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