ArticleMethodsX2020
A targeted mass spectrometry method for the accurate label-free quantification of immunogenic gluten peptides produced during simulated digestion of food matrices.
Article in MethodsX, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Improved multi-food allergen analysis of processed foods using HRAM-LC-MS/MS with an ELISA-validated extraction solution and MS sample prep kit.Analytical and bioanalytical chemistry · 2024Article
- Investigating the Formation of In Vitro Immunogenic Gluten Peptides after Covalent Modification of Their Structure with Green Tea Phenolic Compounds under Alkaline Conditions.Journal of agricultural and food chemistry · 2024Article
- Editorial overview: Virtual collection on chromatographic and mass spectrometric methods in food, health, and agriculture.MethodsX · 2022Article
- Analytical and functional approaches to assess the immunogenicity of gluten proteins.Frontiers in nutrition · 2022Review
- A Case Study of the Response of Immunogenic Gluten Peptides to Sourdough Proteolysis.Nutrients · 2021Article
Corrections and comments
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Authors and funding
7 authors.
Funding
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Abstract
Mass spectrometry (MS) is an emerging method to determine the accurate concentration of immunogenic gluten peptides. It is of interest to quantify specific peptides within the gluten peptidome due to the role they play in the activation of the celiac immune cascade. Celiac disease is an autoimmune disorder triggered in genetically susceptible individuals by the presence of specific gluten peptides that resist digestion in the gastrointestinal tract. The protocol detailed within this paper can accurately quantify (label-free) the concentration of six immunogenic gluten peptides (including the 33mer) released from a food matrix using the INFOGEST
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