Mass spectrometry analysis of gliadins in celiac disease.
In recent years, scientific research on wheat gluten proteins has followed three main directions aimed at (1) finding relationships between individual genetic alleles coding for gliadins, high or low molecular weight glutenin subunits, and the viscoelastic dough properties of flour-derived products such as pasta and bread; (2) identifying prolamins and derived peptides involved in celiac disease, a pathological condition in which the small intestine of genetically predisposed individuals is reversibly damaged; and (3) developing and validating sensitive and specific methods for detecting trace amounts of gluten proteins in gluten-free foods for celiac disease patients. In this review, the main aspects of current and perspective applications of mass spectrometry and proteomic technologies to the structural characterization of gliadins are presented, with focus on issues related to detection, identification, and quantification of intact gliadins, as well as gliadin-derived peptides relevant to the biochemical, immunological, and toxicological aspects of celiac disease.
Ferranti
Pasquale
P
Dipartimento di Scienza degli Alimenti, University of Naples Federico II, Parco Gussone, Portici I- 80055, Italy. ferranti@unina.it
Mamone
Gianfranco
G
Picariello
Gianluca
G
Addeo
Francesco
F
D002446:Celiac Disease / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D000939:Epitopes / Q000032:analysis; D005285:Fermentation; D005504:Food Analysis; D005903:Gliadin / Q000032:analysis* / Q000633:toxicity; D006801:Humans; D013058:Mass Spectrometry; D040901:Proteomics; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D011503:Transglutaminases / Q000737:chemistry / Q000378:metabolism
D000939:Epitopes; D005903:Gliadin; D011503:Transglutaminases