Susceptibility to transglutaminase of gliadin peptides predicted by a mass spectrometry‐based assay

FEBS Letters

Ferranti, Pasquale¹  Tafuro, Filomena¹  Addeo, Francesco¹  Melck, Dominique¹  Chianese, Lina²  Longobardo, Luigi¹  Mamone, Gianfranco¹ 

[1] Istituto di Scienze dell'Alimentazione del CNR, Avellino, Italy;Dipartimento di Scienza degli Alimenti, Università degli Studi di Napoli ‘Federico II’, Portici, Italy

关键词: Transglutaminase;    Celiac disease;    Gliadin;    Mass spectrometry;    Peptidomics;    tTG;    tissue transglutaminase;    CD;    celiac disease;    PT digest;    pepsin–trypsin digest;    MDC;    monodansylcadaverine;    LC/MS;    liquid chromatography-electrospray mass spectrometry;    nES-MS/MS;    nano-ES tandem mass spectrometry;   

DOI  :  10.1016/S0014-5793(04)00231-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown