Peanut Allergen Ara h 1 Interacts with Proanthocyanidins into Higher Molecular Weight Complexes
| العنوان: | Peanut Allergen Ara h 1 Interacts with Proanthocyanidins into Higher Molecular Weight Complexes |
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| المؤلفون: | Harry Gruppen, Jean-Paul Vincken, E.L. van Boxtel, L.A.M. van den Broek, S.J. Koppelman |
| المساهمون: | TNO Kwaliteit van Leven |
| المصدر: | Journal of Agricultural and Food Chemistry, 21, 55, 8772-8778 Journal of Agricultural and Food Chemistry, 55(21), 8772-8778 Journal of Agricultural and Food Chemistry 55 (2007) 21 |
| سنة النشر: | 2007 |
| مصطلحات موضوعية: | glycoprotein, Models, Molecular, Glycine max, major proteins, glycinin, Trimer, soybean protein, cupin superfamily, soybean seeds, Legumin, Drug Interactions, vegetable protein, proanthocyanidin, Soy protein, Plant Proteins, degradation, chemistry.chemical_classification, mechanisms, Ara, biology, Food Chemistry, Seed Storage Proteins, article, food and beverages, Ara h 1 protein, Arachis hypogaea, ion exchange chromatography, Chromatography, Ion Exchange, Biochemistry, Proanthocyanidin, Chromatography, Gel, Soybean Proteins, Protein-polyphenol interaction, lipids (amino acids, peptides, and proteins), General Agricultural and Biological Sciences, h-i, allergen, beta-conglycinin, Peanut allergy, Globulin, gel chromatography, Chemical structure, chemistry, globulin, Food technology, Arachis hypogaea, BBP Sustainable Chemistry & Technology, Ara h 1, Levensmiddelenchemie, Proanthocyanidins, Glycoproteins, VLAG, drug interaction, protein complexes, Molecular mass, ige-binding, Membrane Proteins, molecular weight, Globulins, General Chemistry, Antigens, Plant, Allergens, biochemical phenomena, metabolism, and nutrition, carbohydrates (lipids), chemical structure, biology.protein, Glycoprotein, beta conglycinin protein, Glycine max, beta-conglycinin protein, Glycine max |
| الوصف: | Mildly extracted peanut allergen Ara h 1 was previously reported to occur as an oligomeric complex. In this paper we describe how the protein in this oligomeric complex interacts noncovalently with phenolic compounds of the proanthocyanidin type. These interactions are being disrupted during anion exchange chromatography, resulting in the dissociation of the oligomeric Ara h 1 complex into protein trimers. By use of the known three-dimensional structure of ß-conglycinin, a soy protein homologous to Ara h 1, proline-rich regions were observed in silico on both faces of its trimeric structure, which are conserved in Ara h 1. These proline-rich regions could explain the binding of proanthocyanidins to Ara h 1 and the formation of multiple Ara h 1 trimer complexes. This was supported by the observation that the addition of peanut proanthocyanidins to trimeric Ara h 1 and to ß-conglycinin resulted in the formation of soluble oligomeric protein complexes. The structurally related legumin proteins do not contain such proline-rich regions on both sides of the protein, and proanthocyanidins were shown to have a lower affinity for legumin proteins from peanuts and soybeans (peanut allergen Ara h 3 and soy glycinin, respectively). Ara h 1 present as the oligomeric complex is assumed to be the representative form of the allergen in which it is consumed by humans. Keywords: Peanut allergy; Ara h 1; protein-polyphenol interaction; proanthocyanidins. |
| وصف الملف: | application/octet-stream; application/pdf |
| اللغة: | English |
| تدمد: | 0021-8561 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77c0a00c8600db3a3f451f841b345568Test https://doi.org/10.1021/jf071585kTest |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....77c0a00c8600db3a3f451f841b345568 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 00218561 |
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