Abstract
This study aimed to identify the potential allergenic peptides and critical amino acids derived from the digestive products of glycated α-lactalbumin. Degranulation assays showed that amino acid sequences (AA) 37–50, AA80-90, AA94-104 and AA115-123 obtained from its digestive products were still allergenic, and AA94-104 was identified as the potential allergenic peptide because it showed the highest release level of β-hexosaminidase, interleukin-6 and histamine. Molecular docking indicated that all of the four peptides could interact with MHC class Ⅱ by hydrophobic interactions and hydrogen bonds. Molecular dynamic simulation confirmed that binding with AA94-104 led to MHC class Ⅱ being more compact. Therefore, AA94-104 might be the potential allergenic peptide. Allergenicity analysis and molecular docking indicated that leucine96, isoleucine101, asparagine102 and tryptophan104 might be the critical amino acids of AA94-104, due to the lowest allergenicity found in corresponding mutated peptides. These results will provide theoretical guidance for the preparation of hypoallergenic dairy products.
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