Evidence map›Paper›PMID 30710207›Full record

ArticleAnalytical and bioanalytical chemistry2019

Toward an efficient workflow for the analysis of the human milk peptidome.

Kelly A Dingess, Henk W P van den Toorn, Marko Mank, Bernd Stahl, Albert J R Heck

Abstract read
In one paragraph

Article in Analytical and bioanalytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Monitoring Human Milk β-Casein Phosphorylation andInternational journal of molecular sciences · 2021
    Article
  10. Review
  11. Article
  12. Observational
  13. Article
  14. Article
  15. Article
  16. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Kelly A DingessBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, 3584 CH, Utrecht, The Netherlands.
Henk W P van den ToornBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, 3584 CH, Utrecht, The Netherlands.
Marko MankEarly Life Nutrition, Danone Nutricia Research, Uppsalalaan 12, 3584 CT, Utrecht, The Netherlands.
Bernd StahlEarly Life Nutrition, Danone Nutricia Research, Uppsalalaan 12, 3584 CT, Utrecht, The Netherlands.
Albert J R HeckBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, 3584 CH, Utrecht, The Netherlands. a.j.r.heck@uu.nls.

Funding

European Union?s Horizon 2020 research and innovation programme 686547 (MSMed)Netherlands Organization for Scientific Research Proteins@Work (project 184.032.201)
6 · The paper itself

Abstract

There is a growing interest for investigating endogenous peptides from human biofluids which may provide yet unknown functional benefits or provide an early indication of disease states as potential biomarkers. A major technical bottleneck in the investigation of endogenous peptides from body fluids, e.g., serum, urine, saliva, and milk, is that each of these fluids seems to require unique workflows for peptide extraction and analysis. Thus, protocols optimized for serum cannot be directly translated to milk. One biofluid that is readily available, but which has not been extensively explored, is human milk, whose analysis could contribute to our understanding of the immune development of the newborn infant. Due to the occurrence of highly abundant lipids, proteins, and saccharides, milk peptidomics requires dedicated sample preparation steps. The aim of this study was to develop a time and cost-efficient workflow for the analysis of the human milk peptidome, for which we compared peptide extraction methodologies and peptide fragmentation methods. A method using strong acid protein precipitation and analysis by collision-induced dissociation fragmentation was found to be superior to all other test methods, allowing us qualitative and quantitative detection of about 4000 endogenous human milk peptides in a total analysis time of just 18 h.

Indexed as

Amino Acid SequenceChemical PrecipitationChromatography, High Pressure LiquidHumansLiquid-Liquid ExtractionMilk, HumanMilk ProteinsPeptide FragmentsPeptidesProteomicsTandem Mass SpectrometryWorkflowMilk ProteinsPeptide FragmentsPeptidesBiofluidsBiomarker discoveryEndogenous peptidesHuman milkPeptidomics

Identifiers

PMID30710207
PMCPMC6449315

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LicenceCC BY
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Registered trials

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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.