MassIVE MSV000087464

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Monitoring Beta-casein phosphorylation and O-glycosylation over lactation reveals distinct differences between the proteome and endogenous peptidome

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Description

Human milk is a vital biofluid containing a myriad of molecular components to ensure an infants best start at a healthy life. One key component of human milk is Beta-casein, a protein which is not only a structural constituent of casein micelles but also a source of bioactive, often antimicrobial, peptides contributing to milks endogenous peptidome. Importantly, post-translational modifications (PTMs) like phosphorylation and glycosylation typically affect the function of proteins and peptides, but here our understanding of Beta-casein is critically limited. To uncover the scope of proteoforms and endogenous peptidoforms we utilized mass spectrometry (LC-MSMS) to achieve in-depth longitudinal profiling of Beta-casein from human milk, studying two donors across 16 weeks of lactation. We not only observed changes in Beta-caseins known protein and endogenous peptidome phosphorylation, but also in previously unexplored O-glycosylation. This newly discovered PTM of Beta-casein may be important as it resides on known Beta-casein-derived antimicrobial peptide sequences. [doi:10.25345/C51F9Q] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Human milk ; Mass Spectrometry ; O-Glycosylation ; Peptidomics ; Antimicrobial peptides

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Principal Investigators:
(in alphabetical order) 		Albert J.R. Heck, Biomolecular Mass Spectrometry and Proteomics groups, Utrecht University, N/A
Submitting User: Kelly_Dingess_88
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