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 technology
Ara h 1
Peanut allergy
Proanthocyanidins
Protein-polyphenol interaction
allergen
Ara h 1 protein, Arachis hypogaea
beta conglycinin protein, Glycine max
beta-conglycinin protein, Glycine max
globulin
glycinin
glycoprotein
proanthocyanidin
soybean protein
vegetable protein
article
chemical structure
chemistry
drug interaction
gel chromatography
ion exchange chromatography
molecular weight
Allergens
Chromatography, Gel
Chromatography, Ion Exchange
Drug Interactions
Globulins
Glycoproteins
Models, Molecular
Molecular Weight
Plant Proteins
Proanthocyanidins
Soybean Proteins
Ara
Arachis hypogaea
Glycine 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