ArticleMolecular & cellular proteomics : MCP2014
Mechanistic peptidomics: factors that dictate specificity in the formation of endogenous peptides in human milk.
Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 81 citations in OpenAlex.
- Selective Human-Milk-Inspired Antimicrobial Peptides for the Treatment of Bacterial Vaginosis.Pharmaceutics · 2026Article
- Comparative inactivation ofFrontiers in microbiology · 2026Article
- Dynamic Variations in Endogenous Peptides in Chinese Human Milk Across Lactation and Geographical Regions.Nutrients · 2025Article
- Bioactive milk peptides: an updated comprehensive overview and database.Critical reviews in food science and nutrition · 2024Review
- Optimizing workflow efficiency for analyzing low molecular weight endogenous peptides in colostrum.RSC advances · 2024Article
- Proteomic Analysis ofPlants (Basel, Switzerland) · 2024Article
- Network analysis of the proteome and peptidome sheds light on human milk as a biological system.Scientific reports · 2024Article
- Fingerprinting of Proteases, Protease Inhibitors and Indigenous Peptides in Human Milk.Nutrients · 2023Article
- Identification of Potential Bioactive Peptides in Sheep Milk Kefir through Peptidomic Analysis at Different Fermentation Times.Foods (Basel, Switzerland) · 2023Article
- Ecologies, synergies, and biological systems shaping human milk composition-a report from "Breastmilk Ecology: Genesis of Infant Nutrition (BEGIN)" Working Group 2.The American journal of clinical nutrition · 2023Article
- Article
- Proteomics Characterization of Food-Derived Bioactive Peptides with Anti-Allergic and Anti-Inflammatory Properties.Nutrients · 2022Review
- Exploring Human Milk Dynamics: Interindividual Variation in Milk Proteome, Peptidome, and Metabolome.Journal of proteome research · 2022Article
- CLIP-170S is a microtubule +TIP variant that confers resistance to taxanes by impairing drug-target engagement.Developmental cell · 2021Article
- Three Distinct Proteases Are Responsible for Overall Cell Surface Proteolysis in Streptococcus thermophilus.Applied and environmental microbiology · 2021Article
- Monitoring Human Milk β-Casein Phosphorylation andInternational journal of molecular sciences · 2021Article
- Bringing New Methods to the Seed Proteomics Platform: Challenges and Perspectives.International journal of molecular sciences · 2020Review
- Gene-Specific Control of tRNA Expression by RNA Polymerase II.Molecular cell · 2020Article
- Peptidomic Analysis of Urine from Youths with Early Type 1 Diabetes Reveals Novel Bioactivity of Uromodulin PeptidesMolecular & cellular proteomics : MCP · 2020Article
- Alternate RNA Structures.Cold Spring Harbor perspectives in biology · 2020Review
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
An extensive mass spectrometry analysis of the human milk peptidome has revealed almost 700 endogenous peptides from 30 different proteins. Two in-house computational tools were created and used to visualize and interpret the data through both alignment of the peptide quasi-molecular ion intensities and estimation of the differential enzyme participation. These results reveal that the endogenous proteolytic activity in the mammary gland is remarkably specific and well conserved. Certain proteins-not necessarily the most abundant ones-are digested by the proteases present in milk, yielding endogenous peptides from selected regions. Our results strongly suggest that factors such as the presence of specific proteases, the position and concentration of cleavage sites, and, more important, the intrinsic disorder of segments of the protein drive this proteolytic specificity in the mammary gland. As a consequence of this selective hydrolysis, proteins that typically need to be cleaved at specific positions in order to exert their activity are properly digested, and bioactive peptides encoded in certain protein sequences are released. Proteins that must remain intact in order to maintain their activity in the mammary gland or in the neonatal gastrointestinal tract are unaffected by the hydrolytic environment present in milk. These results provide insight into the intrinsic structural mechanisms that facilitate the selectivity of the endogenous milk protease activity and might be useful to those studying the peptidomes of other biofluids.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.