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The human milk peptidome: exploring network insights

ABSTRACT: The aim of this study was to investigate associations among peptides, among proteins, and between peptides and proteins in human milk.

INSTRUMENT(S): Q Exactive HF-X

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Sjef Boeren

LAB HEAD: Sjef Boeren

PROVIDER: PXD036477 | Pride | 2024-05-23

REPOSITORIES: Pride

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			Action	DRS
	MQresult_PD221-PD576.zip	Other
	PD221_Block1-1.raw	Raw
	PD222_Block1-2.raw	Raw
	PD223_Block1-3.raw	Raw
	PD224_Reference1.raw	Raw

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Publications

Network analysis of the proteome and peptidome sheds light on human milk as a biological system.

Dekker Pieter M PM Boeren Sjef S Saccenti Edoardo E Hettinga Kasper A KA

Scientific reports 20240330 1

Proteins and peptides found in human milk have bioactive potential to benefit the newborn and support healthy development. Research has been carried out on the health benefits of proteins and peptides, but many questions still need to be answered about the nature of these components, how they are formed, and how they end up in the milk. This study explored and elucidated the complexity of the human milk proteome and peptidome. Proteins and peptides were analyzed with non-targeted nanoLC-Orbitrap ...[more]

PMID: 38555284

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Human milk dynamics: Inter-individual variation in peptidome

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Project description:Variations in endogenous peptide profiles, functionality, and the enzymes responsible for the formation of these peptides in human milk are understudied. Additionally, there is a lack of knowledge regarding peptides in donor human milk, which is used to feed preterm infants when mother’s own milk is not (sufficiently) available. To assess this, 29 human milk samples from the Dutch Human Milk Bank were analyzed as three groups, preterm late lactation stage (LS) (n=12), term early (n=8) and term late LS (n=9). Gestational age (GA) groups were defined as preterm (24-36 weeks) and term (>37 weeks). LS was determined as days postpartum as early (16-36 days) or late (55-88 days). Peptides, analyzed by LC-MS/MS, and parent proteins (proteins from matched peptide sequences) were identified and quantified, after which peptide functionality and the enzymes responsible for protein cleavage were determined. A total of 16 different parent proteins were identified from human milk, with no differences by GA or LS. We identified 1104 endogenous peptides, of which, the majority were from the parent proteins β-casein, polymeric immunoglobulin receptor, αs1-casein, osteopontin, and κ-casein. The absolute number of peptide differed by GA and LS with 30 and 41 differing sequences respectively (p<0.05) Odds likelihood tests determined that 32 peptides had a predicted bioactive functionality, with no significant differences between groups. Enzyme prediction analysis showed that plasmin/trypsin enzymes most likely cleaved the identified human milk peptides. These results explain some of the variation in endogenous peptides in human milk, leading to future targets that may be studied for functionality.

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Project description:The question whether and which non-human peptides or proteins are present in human milk was raised many decades ago. However, due to cross-reactivity or nonspecific antibody recognition, the accuracy of detection by immunochemical methods has been a concern. Additionally, the relative low-abundance of non-human peptides/proteins in the complex milk sample makes them a challenging target to detect. Here, by deep proteome profiling we detected several non-human peptides, which could be grouped as non-human proteins. We next estimated their concentration in human milk by combining data-dependent shotgun proteomics and parallel reaction monitoring. First, we fractionated human milk at the protein level by using sodium dodecyl sulfate polyacrylamide gel electrophoresis followed by reduction, alkylation and in-gel digestion. The resulted peptide mixtures were subjected to proteomics analysis. We were able to detect 1577 human proteins in human milk. Additionally, we identified 109 non-human peptides, of which 71 were grouped in to 36 non-human proteins. In the next step, we targeted 37 non-human peptides and 9 of them could be repeatedly quantified in human milk samples. Peptides/proteins originating from bovine milk products were the dominant non-human proteins observed, notably bovine caseins (α-S1-, α-S2-, β-, κ-caseins) and β-lactoglobulin.

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2023-10-09 | PXD037629 | Pride

Peptidomics analysis of milk protein-derived peptides released over time in the preterm infant stomach

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