Evidence map›Paper›PMID 41603960›Full record

ArticleAnalytical and bioanalytical chemistry2026

Integrated targeted and untargeted analysis of polar peptides in foods using hydrophilic interaction liquid chromatography-data-independent acquisition-mass spectrometry.

Boudewijn Hollebrands, Germaine Thong, Hans-Gerd Janssen

Abstract read
In one paragraph

Article in Analytical and bioanalytical chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Boudewijn HollebrandsUnilever Foods Innovation Centre-Hive, Bronland 14, 6708 WH, Wageningen, the Netherlands. boudewijn.hollebrands@unilever.com.
Germaine ThongUnilever Foods Innovation Centre-Hive, Bronland 14, 6708 WH, Wageningen, the Netherlands.
Hans-Gerd JanssenUnilever Foods Innovation Centre-Hive, Bronland 14, 6708 WH, Wageningen, the Netherlands.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A hydrophilic interaction liquid chromatography-data-independent acquisition mass spectrometry (HILIC-DIA-MS) workflow was developed for simultaneous targeted semi-quantification of polar peptides and untargeted profiling of both peptides and other polar compounds in complex food matrices. The method uses a zwitterionic HILIC column optimized for separation of short polar peptides that are challenging to retain on reversed-phase columns. Many of these peptides contain charged amino acids and contribute to basic taste modalities such as umami and saltiness. Both targeted peptide analysis and comprehensive untargeted profiling were achieved by applying DIA-MS detection. This data acquisition mode was shown to be reproducible and sensitive while enabling retrospective data processing. High-resolution MS1 scans (60.000 FWHM), combined with fast MS2 scans and DIA mass windows of 15 m/z yielded highly repeatable and selective LC-MS profiles, allowing differentiation of structural isomers (e.g., alpha-glutamyl (umami) and gamma-glutamyl (kokumi)). The method was validated using taste-relevant dipeptides, demonstrating low detection limits (0.1-0.9 µM), good intra-day and inter-day precision, and high recovery (96%) in commercial soy sauce and yeast extract matrices. The workflow was further applied to the relative quantification of peptides and the untargeted profiling of characteristic molecular features in cheese, ham, and extracts from dried food ingredients. The integration of targeted and untargeted analyses demonstrates the suitability of HILIC-DIA-MS for comprehensive characterization of polar compounds in food systems.

Indexed as

Food AnalysisLiquid Chromatography-Mass SpectrometryMass SpectrometryPeptidesChromatography, LiquidHydrophobic and Hydrophilic InteractionsLimit of DetectionReproducibility of ResultsPeptidesFood peptidesHILIC-DIA-MSPolar bioactive compoundsRetrospective analysisUntargeted profiling

Identifiers

PMID41603960
PMCPMC13144269

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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.