Peanut
allergy is a prevalent and concerning food allergy. Roasting
can introduce structural changes to peanut allergens, affecting their
allergenicity, but the structure on the primary structure is unclear.
Here, the breakage sites were identified by mass spectrometry and
software tools, and structural changes were simulated by molecular
dynamics and displayed by PyMOL software. Results revealed that the
appearance frequencies of L, Q, F, and E were high at the N-terminal
of the breakage site, while S and E were dominant at the C-terminal.
In the conformational structure, breakage sites were found close to
disulfide bonds and the Cupin domains of Ara h 1 and Ara h 3. The
breakage of allergens destroyed linear epitopes and might change the
conformation of epitopes, which could influence peanuts’ potential
allergenicity.