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 leucine, isoleucine, asparagine and tryptophan 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.

中文翻译：

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通过致敏性评价和分子动力学模拟研究糖化α-乳清蛋白消化产物中潜在致敏肽和关键氨基酸

本研究旨在鉴定源自糖化 α-乳清蛋白消化产物的潜在过敏肽和关键氨基酸。脱颗粒试验表明，从其消化产物中获得的氨基酸序列（AA）37-50、AA80-90、AA94-104和AA115-123仍然具有致敏性，其中AA94-104被确定为潜在的致敏肽，因为它表现出最高的致敏性。 β-己糖胺酶、白细胞介素 6 和组胺的释放水平。分子对接表明4种肽均能通过疏水作用和氢键与MHC II类相互作用。分子动力学模拟证实，与AA94-104结合导致MHC Ⅱ类更加紧凑。因此，AA94-104可能是潜在的致敏肽。过敏性分析和分子对接表明，亮氨酸、异亮氨酸、天冬酰胺和色氨酸可能是 AA94-104 的关键氨基酸，因为在相应的突变肽中发现了最低的过敏性。这些结果将为低过敏性乳制品的制备提供理论指导。