Phosphorylation is an important post-translational modification that affects protein function and biological processes. In this study, label-free quantitative phosphoproteomics was employed to systematically identify the phosphorylated proteins and their phosphorylation sites in human colostrum (HC) and mature milk (HM) whey. In human colostrum, 30 phosphorylation sites on 24 phosphoproteins were identified, whereas in mature milk, 9 phosphorylation sites on 8 phosphoproteins were detected. Functional analysis revealed that the phosphorylated proteins in colostrum were primarily involved in immune regulation and inflammatory responses, while those in mature milk were more associated with metabolic regulation and immune homeostasis to meet the nutritional and physiological needs of infants during later stages of development. These findings highlight the dynamic adaptability of breast milk components according to the developmental needs of the infant, providing an important scientific basis for the design of stage-specific infant formula.

中文翻译：

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人初乳和成熟乳中乳清蛋白的磷酸化动力学比较：对婴儿营养的影响

磷酸化是一种重要的翻译后修饰，影响蛋白质功能和生物过程。在这项研究中，采用无标记定量磷酸化蛋白质组学系统鉴定人初乳 （HC） 和成熟乳 （HM） 乳清中的磷酸化蛋白及其磷酸化位点。在人初乳中，鉴定出 24 种磷蛋白上的 30 个磷酸化位点，而在成熟乳中，检测到 8 种磷蛋白上的 9 个磷酸化位点。功能分析显示，初乳中的磷酸化蛋白主要参与免疫调节和炎症反应，而成熟乳中的磷酸化蛋白更多地与代谢调节和免疫稳态相关，以满足婴儿发育后期的营养和生理需求。这些发现突出了母乳成分根据婴儿发育需要的动态适应性，为特定阶段婴儿配方奶粉的设计提供了重要的科学依据。