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Article Abstract
The mechanism of PEF treatment (5-20 kV/cm for 0.5-2 h) changing spatial conformation and enhancing allergenicity of parvalbumin of grass carp was clarified, and molecular dynamics simulations (MDS) was utilized to explore hot-spot residues and epitopes of parvalbumin-IgE complex. The phenomenon revealed that the IgG and IgE binding capacity of parvalbumin maximally enhanced by 37.24 % and 27.63 % respectively, but subsequently decreased after 20 kV/cm exposure for 1 h. Atomic force microscope showed that the particle morphology of PEF-treated parvalbumin became more regular and homogeneous, with dissociation of aggregates due to decreased hydrophobic interaction. Furthermore, 5-20 kV/cm treatments promoted conformation unfolded and de-spiralization, rendering it easy for target antibodies to interact with related epitopes. MDS showed that the critical epitopes between parvalbumin and IgE were phenylalanine58, glutamate60-61, aspartate91, aspartate93-glycine96 and glutamate102 with ΔG < -1 kcal/mol, and hot-spot residues were phenylalanine, glutamate and aspartate with ΔΔG > 1 kcal/mol.
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| http://dx.doi.org/10.1016/j.foodchem.2025.145916 | DOI Listing |
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