Proteomics

Dataset Information

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


ABSTRACT: Over the course of milk digestion, native milk proteases and infant digestive proteases fragment intact proteins into peptides with potential bioactivity. This study investigated the release of peptides over three hours of gastric digestion in 14 preterm infant sample sets. The peptide content was extracted and analyzed from milk and gastric samples via Orbitrap tandem mass spectrometry. The relative ion intensity (abundance) and count of peptides in each sample were compared over time and between infants fed milk fortified with bovine milk fortifier and infants fed unfortified milk. Bioactivity of the identified peptides was predicted by sequence homology to known bioactive milk peptides. Both total and bioactive peptide abundance and count continuously increased over three hours of gastric digestion. After accounting for infant weight, length, and post-conceptual age, fortification of milk limited the release of peptides from human milk proteins. Peptides that survived further gastric digestion after their initial release were structurally more similar to bioactive peptides than non-surviving peptides. This work is the first to provide a comprehensive profile of milk peptides released during gastric digestion over time, which is an essential step in determining which peptides are most likely to be biologically relevant in the infant.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human) Bos Taurus (bovine)

TISSUE(S): Milk

SUBMITTER: Robert Beverly  

LAB HEAD: David Dallas

PROVIDER: PXD012192 | Pride | 2019-03-12

REPOSITORIES: pride

Dataset's files

Source:
Action DRS
042517_DD15_Milk.raw Raw
042517_DD16_Milk.raw Raw
042517_DD17Milk.raw Raw
042517_DD18_19_Milk.raw Raw
042517_DD20_Milk.raw Raw
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Publications

Peptidomics Analysis of Milk Protein-Derived Peptides Released over Time in the Preterm Infant Stomach.

Beverly Robert L RL   Underwood Mark A MA   Dallas David C DC  

Journal of proteome research 20190124 3


Over the course of milk digestion, native milk proteases and infant digestive proteases fragment intact proteins into peptides with potential bioactivity. This study investigated the release of peptides over 3 h of gastric digestion in 14 preterm infant sample sets. The peptide content was extracted and analyzed from milk and gastric samples via Orbitrap tandem mass spectrometry. The relative ion intensity (abundance) and count of peptides in each sample were compared over time and between infan  ...[more]

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