Publication: Research - peer-review › Journal article – Annual report year: 2012
The major peanut allergen Ara h 1 is an easily digestible protein under physiological conditions. The present study revealed that pepsin digestion products of Ara h 1 retained the sensitizing potential in a Brown Norway rat model, while this sensitizing capacity was lost by separating the digest into fractions by gel permeation chromatography. Protein chemical analysis showed that the peptide composition as well as the aggregation profiles of the fractions of Ara h 1 digest differed from that of the whole pool. These results indicate that the sensitizing capacity of digested Ara h 1 is a consequence of the peptides being in an aggregated state resembling the intact molecule or that most peptides of the digests need to be present in the same solution, having a synergistic or adjuvant effect and thereby augmenting the immune response against other peptides.
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- AGRICULTURE, CHEMISTRY, FOOD, MAJOR PEANUT ALLERGEN, B-CELL EPITOPES, STRUCTURE-IMMUNOGENICITY RELATIONSHIP, IGE-BINDING EPITOPES, FOOD ALLERGENS, SYNTHETIC PEPTIDES, IN-VITRO, GASTROINTESTINAL DIGESTION, MILK-PROTEINS, ANTIBODIES