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dc.contributor.authorMattison, Christopher Pen_US
dc.contributor.authorDinter, Jensen_US
dc.contributor.authorBerberich, Matthew Jen_US
dc.contributor.authorChung, Si-Yinen_US
dc.contributor.authorReed, Shawndrika Sen_US
dc.contributor.authorLe Gall, Sylvieen_US
dc.contributor.authorGrimm, Casey Cen_US
dc.date.accessioned2015-09-01T13:28:39Z
dc.date.issued2015en_US
dc.identifier.citationMattison, Christopher P, Jens Dinter, Matthew J Berberich, Si-Yin Chung, Shawndrika S Reed, Sylvie Le Gall, and Casey C Grimm. 2015. “In vitro evaluation of digestive and endolysosomal enzymes to cleave CML-modified Ara h 1 peptides.” Food Science & Nutrition 3 (4): 273-283. doi:10.1002/fsn3.215. http://dx.doi.org/10.1002/fsn3.215.en
dc.identifier.issn2048-7177en
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:21462597
dc.description.abstractAra h 1 is a major peanut allergen. Processing-induced modifications may modulate the allergenic potency of Ara h 1. Carboxymethyl lysine (CML) modifications are a commonly described nonenzymatic modification on food proteins. In the current study, we tested the ability of digestive and endolysosomal proteases to cleave CML-modified and unmodified Ara h 1 peptides. Mass spectrometric analyses of the digested peptides demonstrate that carboxymethylation of lysine residues renders these peptides refractory to trypsin digestion. We did not detect observable differences in the simulated gastric fluid or endolysosomal digestion between the parental and CML-modified peptides. One of the tested peptides contains a lysine residue previously shown to be CML modified laying in a previously mapped linear IgE epitope, but we did not observe a difference in IgE binding between the modified and parental peptides. Our findings suggest a molecular mechanism for the increased resistance of peanut allergens modified by thermal processing, such as Ara h 1, to digestion in intestinal fluid after heating and could help explain how food processing-induced modifications may lead to more potent food allergens by acting to protect intact IgE epitopes from digestion by proteases targeting lysine residues.en
dc.language.isoen_USen
dc.publisherJohn Wiley & Sons, Ltden
dc.relation.isversionofdoi:10.1002/fsn3.215en
dc.relation.hasversionhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC4534154/pdf/en
dash.licenseLAAen_US
dc.subjectAra h 1en
dc.subjectcarboxymethyl lysineen
dc.subjectMaillard reactionen
dc.subjectmass spectrometryen
dc.subjectpeptideen
dc.subjectproteolysisen
dc.titleIn vitro evaluation of digestive and endolysosomal enzymes to cleave CML-modified Ara h 1 peptidesen
dc.typeJournal Articleen_US
dc.description.versionVersion of Recorden
dc.relation.journalFood Science & Nutritionen
dash.depositing.authorLe Gall, Sylvieen_US
dc.date.available2015-09-01T13:28:39Z
dc.identifier.doi10.1002/fsn3.215*
dash.contributor.affiliatedLe Gall, Sylvie


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