For over 200 million years, lactation has co-evolved with mammalian infants to provide nourishment. Many milk proteins lack known function intact. Historically, these proteins were thought to serve only as an amino acid source for infant growth. We theorized that milk proteins fragments (peptides) released through digestion within the mammary gland and in the infant would be functional.  With state-of-the-art liquid chromatography-mass spectrometry and bioinformatics, we discovered hundreds of naturally occurring peptides in human and bovine milk and hundreds of newly released peptides in the infant stomach. Our bioinformatic analyses demonstrate that proteases produced within the mammary gland are responsible for cleavage in milk and continue to control digestion within the infant stomach. Many of the released peptides are homologous with known antimicrobial peptides and, as an ensemble, these peptides inhibit the growth of several pathogenic bacteria. We suspect these antimicrobials are pathogen-specific, which could lead to translational applications.

Milk peptidomics across infant digestion

248th National Meeting (2014)

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