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Fac-simile Scheda Linee di Ricerca - Federalimentare

Fac-simile Scheda Linee di Ricerca - Federalimentare

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Dati pubblicati inerenti il tema <strong>di</strong> ricerca:1. Mamone G, Ferranti P, Rossi M, Roepstorff P, Fierro O, Malorni A, Addeo F. Identificationof a peptide from alpha-glia<strong>di</strong>n resistant to <strong>di</strong>gestive enzymes: implications for celiac <strong>di</strong>sease.J Chromatogr. B 855:236-2341, 2007Current knowledge in<strong>di</strong>cates that both innate and adaptive immune responses are involved in Celiac <strong>di</strong>sease(CD) driven by <strong>di</strong>fferent glia<strong>di</strong>n peptides. By studyinga representative recombinant alpha-glia<strong>di</strong>n form, a further25-mer peptide resistant to gastric, pancreatic, and human intestinal brush-border membrane enzymes was detected.This peptide latter encompasses the sequence 31-43 known to elicit the innate immune response in CD.The resistance of 25-mer, as well as that of the already described 33-mer related to the CD adaptive immune response,was confirmed on a standard flour wheat sample representative of the mostwidespread European varieties.2. Ferranti P, Mamone G, Picariello G, Addeo F. Mass spectrometry analysis of glia<strong>di</strong>ns in celiac<strong>di</strong>sease. J Mass Spectrom. 42:1531-1548, 2007In recent years, scientific research on wheat gluten proteins has followed three main <strong>di</strong>rections aimed at (1) fin<strong>di</strong>ngrelationships between in<strong>di</strong>vidual genetic alleles co<strong>di</strong>ng for glia<strong>di</strong>ns, high or low molecular weight gluteninsubunits, and the viscoelastic dough properties of flour-derived products such as pasta and bread; (2) identifyingprolamins and derived peptides involved in celiac <strong>di</strong>sease, a pathological con<strong>di</strong>tion in which the small intestineof genetically pre<strong>di</strong>sposed in<strong>di</strong>viduals is reversibly damaged; and (3) developing and validating sensitive andspecific methods for detecting trace amounts of gluten proteins in gluten-free foods for celiac <strong>di</strong>sease patients. Inthis review, the main aspects of current and perspective applications of mass spectrometry and proteomic technologiesto the structural characterization of glia<strong>di</strong>ns are presented, with focus on issues related to detection,identification, and quantification of intact glia<strong>di</strong>ns, as well as glia<strong>di</strong>n-derived peptides relevant to the biochemical,immunological, and toxicological aspects of celiac <strong>di</strong>sease.SISTAL - SOCIETA’ ITALIANA DI SCIENZE E TECNOLOGIE ALIMENTARIDipartimento <strong>di</strong> Scienze e Tecnologie Agroalimentari, Università degli Stu<strong>di</strong> della TusciaVia San Camillo de Lellis, 01100 ViterboTel.: 0761- 35 74 94/7 , Fax: 0761- 35 74 98, e-mail: mmoresi@unitus.it285

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