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Susceptibility to transglutaminase of gliadin peptides predicted by a mass spectrometry‐based assay
Author(s) -
Mamone Gianfranco,
Ferranti Pasquale,
Melck Dominique,
Tafuro Filomena,
Longobardo Luigi,
Chianese Lina,
Addeo Francesco
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00231-5
Subject(s) - tissue transglutaminase , gliadin , chemistry , glutenin , trypsin , glutamine , biochemistry , pepsin , tandem mass spectrometry , lysine , deamidation , peptide , chromatography , enzyme , mass spectrometry , gluten , amino acid , protein subunit , gene
A peptidomics approach was developed to identify transglutaminase‐susceptible Q residues within a pepsin–trypsin gliadin digest. Based on tagging with a monodansylcadaverine fluorescent probe, six α/β‐, γ‐gliadin, and low molecular weight glutenin peptides were identified by nanospray tandem mass spectrometry. In functioning as an acyl acceptor, tissue transglutaminase was able to form complexes with the glutamine‐rich gliadin peptides, whereas by lowering pH, the peptides were deamidated by transglutaminase at the same Q residues, which were previously transamidated. The main common feature shared by the peptides was the consensus sequence Q‐X‐P. Our findings offer relevant information for the understanding of how dietary peptides interact with the host organism in celiac disease.