Human milk peptides differentiate between the preterm and term infant and across varying lactational stages

Kelly A. Dingess, Marita de Waard, Sjef Boeren, Jacques Vervoort, Tim T. Lambers, Johannes B. van Goudoever, Kasper Hettinga*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

10 Citations (Scopus)

Abstract

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 peptides 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.
Original languageEnglish
Pages (from-to)3769-3782
JournalFood & Function
Volume8
Issue number10
DOIs
Publication statusPublished - 1 Oct 2017

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Human Milk
breast milk
Premature Infants
peptides
Peptides
lactation stage
Lactation
gestational age
Caseins
Gestational Age
casein
Enzymes
late lactation
Proteins
enzymes
proteins
Milk Banks
Polymeric Immunoglobulin Receptors
osteopontin
Osteopontin

Cite this

Dingess, Kelly A. ; de Waard, Marita ; Boeren, Sjef ; Vervoort, Jacques ; Lambers, Tim T. ; van Goudoever, Johannes B. ; Hettinga, Kasper. / Human milk peptides differentiate between the preterm and term infant and across varying lactational stages. In: Food & Function. 2017 ; Vol. 8, No. 10. pp. 3769-3782.
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abstract = "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 peptides 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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Human milk peptides differentiate between the preterm and term infant and across varying lactational stages. / Dingess, Kelly A.; de Waard, Marita; Boeren, Sjef; Vervoort, Jacques; Lambers, Tim T.; van Goudoever, Johannes B.; Hettinga, Kasper.

In: Food & Function, Vol. 8, No. 10, 01.10.2017, p. 3769-3782.

Research output: Contribution to journalArticleAcademicpeer-review

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AU - Dingess, Kelly A.

AU - de Waard, Marita

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AU - Vervoort, Jacques

AU - Lambers, Tim T.

AU - van Goudoever, Johannes B.

AU - Hettinga, Kasper

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SN - 2042-6496

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