Given that roasting changes the structure and allergenicity of peanut allergens, the structural information of peanut allergens must be expounded to explain the alteration in their allergenicity. This work focused on allergen aggregations (AAs) in roasted peanuts. IgE recognition capability was assessed via western blot analysis. The disulfide bond (DB) rearrangement and chemical modification in AAs were identified by combining mass spectroscopy and software tools, and structural changes induced by cross-links were displayed by molecular dynamics and PyMOL software. Results showed that AAs were strongly recognized by IgE and cross-linked mainly by DBs. The types of DB rearrangement in AAs included interprotein (98 peptide pairs), intraprotein (22 peptide pairs), and loop-linked (6 peptides) DBs. Among allergens, Ara h 2 and Ara h 6 presented the most cysteine residues to cross-linkf with others or themselves. DB rearrangement involved IgE epitopes and induced structural changes. Ara h 1 and Ara h 3 were predominantly chemically modified. Moreover, chemical modification altered the local structures of proteins, which may change the allergenic potential of allergens.
Keywords: aggregation; chemical modification; disulfide bond rearrangement; peanut protein; roast.