Proteomics

Dataset Information

0

Gastrointestinal digestion of hazelnut allergens on molecular level: Elucidation of degradation kinetics and resistant immunoactive peptides using mass spectrometry


ABSTRACT: Allergy to hazelnut seeds ranks among the most prevalent food allergies in Europe. The aim of this study was to elucidate the gastrointestinal digestion of hazelnut allergens on molecular level. Hazelnut flour was digested in vitro following the Infogest consensus model. For six allergenic proteins, the time-dependent course of digestion was monitored by SDS-PAGE and HPLC−MS/MS, and degradation products were characterized by a bottom-up proteomics approach. Depending on the molecular structure, a specific biochemical fate was observed for each allergen, and degradation kinetics were traced back to the peptide level. 1183 peptides were characterized, including 130 peptides that carry known IgE-binding epitopes and may represent sensitizers for hazelnut allergy. The kinetics of peptide formation and degradation were determined by label free quantification and follow a complex multi-stage mechanism.

INSTRUMENT(S): LTQ Orbitrap XL

ORGANISM(S): Corylus Avellana

TISSUE(S): Seed

SUBMITTER: Robin Korte  

LAB HEAD: Jens Brockmeyer

PROVIDER: PXD006412 | Pride | 2017-07-11

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Corylusavellana160226.fasta Fasta
gas1-0min.raw Raw
gas1-10min.raw Raw
gas1-120min.raw Raw
gas1-15min.raw Raw
Items per page:
1 - 5 of 63
altmetric image

Publications

Gastrointestinal digestion of hazelnut allergens on molecular level: Elucidation of degradation kinetics and resistant immunoactive peptides using mass spectrometry.

Korte Robin R   Bräcker Julia J   Brockmeyer Jens J  

Molecular nutrition & food research 20170814 10


<h4>Scope</h4>Allergy to hazelnut seeds ranks among the most prevalent food allergies in Europe. The aim of this study was to elucidate the gastrointestinal digestion of hazelnut allergens on molecular level.<h4>Methods and results</h4>Hazelnut flour was digested in vitro following the Infogest consensus model. For six allergenic proteins, the time-dependent course of digestion was monitored by SDS-PAGE and HPLC-MS/MS, and degradation products were characterized by a bottom-up proteomics approac  ...[more]

Similar Datasets

2022-08-12 | PXD031067 | Pride
2023-10-24 | PXD037801 | Pride
2021-09-09 | PXD021577 | Pride
2011-12-31 | E-GEOD-23685 | biostudies-arrayexpress
2011-09-02 | E-GEOD-31830 | biostudies-arrayexpress
2017-12-14 | PXD008192 | Pride
2022-03-07 | PXD029356 | Pride
2024-08-09 | PXD046332 | Pride
2018-06-26 | PXD005923 | Pride
2023-08-18 | PXD040551 | Pride