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Updated: Jun 14, 2025

LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics
Published on: April 9, 2017
Deamidation modifies gliadin digestion affecting peptide behaviors in self-assembly, mucus permeation, and intestinal
Mingxi Liu1, Liang Dong1, Lijun Yin1
1College of Food Science and Nutritional Engineering, Beijing Key Laboratory of Functional Food from Plant Resources, China Agricultural University, Beijing 100083, China.
Abstract:
Gliadin induces direct intestinal epithelial damage due to the interaction between the intestinal epithelium and gliadin peptides with particular self-assembly properties after digestion. This study explored if and how deamidation affected intestinal epithelial damage. The results demonstrated the alteration of self-assembly that when the degree of deamidation (DD) was less than 20 %, the decrease of peptide length and increase of polarity were the main reasons for the reduction of particle size and spherical nanoparticles. As DD was 26 %, the increase of negative charges was responsible for size increase and shape alteration to linear strands due to the electrostatic attraction. These alterations of self-assembly behaviors facilitated mucus permeation. Deamidated gliadin peptides inhibited the Caco-2 cell damage due to the weakened interaction with the cell membrane. The work demonstrated how deamidation modified the gliadin peptides after digestion in minimizing intestinal epithelial damage, ensuring the safety of deamidation as a modification method.
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