Print Email Facebook Twitter Peanut allergen Ara h 1 interacts with proanthocyanidins into higher molecular weight complexes Title Peanut allergen Ara h 1 interacts with proanthocyanidins into higher molecular weight complexes Author van Boxtel, E.L. van den Broek, L.A.M. Koppelman, S.J. Vincken, J.-P. Gruppen, H. TNO Kwaliteit van Leven Publication year 2007 Abstract 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 β-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 β-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. © 2007 American Chemical Society. Subject Food technologyAra h 1Peanut allergyProanthocyanidinsProtein-polyphenol interactionallergenAra h 1 protein, Arachis hypogaeabeta conglycinin protein, Glycine maxbeta-conglycinin protein, Glycine maxglobulinglycininglycoproteinproanthocyanidinsoybean proteinvegetable proteinarticlechemical structurechemistrydrug interactiongel chromatographyion exchange chromatographymolecular weightAllergensChromatography, GelChromatography, Ion ExchangeDrug InteractionsGlobulinsGlycoproteinsModels, MolecularMolecular WeightPlant ProteinsProanthocyanidinsSoybean ProteinsAraArachis hypogaeaGlycine max To reference this document use: http://resolver.tudelft.nl/uuid:61fa03a1-cd3f-4ec6-978c-79c24b1691b5 DOI https://doi.org/10.1021/jf071585k TNO identifier 240250 ISSN 0021-8561 Source Journal of Agricultural and Food Chemistry, 55 (21), 8772-8778 Document type article Files To receive the publication files, please send an e-mail request to TNO Library.