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Improved short peptide identification using HILIC-MS/MS: retention time prediction model based on the impact of amino acid position in the peptide sequence

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dc.contributor.author Le Maux, Solène
dc.contributor.author Nongonierma, Alice B.
dc.date.accessioned 2017-04-21T10:45:18Z
dc.date.available 2017-04-21T10:45:18Z
dc.date.issued 2015
dc.identifier.uri http://hdl.handle.net/10344/5726
dc.description peer-reviewed en_US
dc.description.abstract Short peptides can have interesting beneficial effects but they are difficult to identify in complex mixtures. We developed a method to improve short peptide identification based on HILIC-MS/MS. The apparent hydrophilicity of peptides was determined as a function of amino acid position in the sequence. This allowed the differentiation of peptides with the same amino acid composition but with a different sequence (homologous peptides). A retention time prediction model was established using the hydrophilicity and peptide length of 153 di- to tetrapeptides. This model was proven to be reliable (R-2 = 0.992), it was validated using statistical methods and a mixture of 14 synthetic peptides. A whey protein hydrolysate was analysed to assess the ability of the model to identify unknown peptides. In parallel to milk protein database and de nova searches, the retention time prediction model permitted reduction and ranking of potential short peptides, including homologous peptides, present in the hydrolysate. (C) 2014 Elsevier Ltd. All rights reserved. en_US
dc.language.iso eng en_US
dc.publisher Elsevier en_US
dc.relation.ispartofseries Food Chemistry;173, pp. 847-854
dc.relation.uri http://doi.org/10.1016/j.foodchem.2014.10.104
dc.rights This is the author’s version of a work that was accepted for publication in Food Chemistry. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Food Chemistry, 173, pp. 847-854, http://doi.org/10.1016/j.foodchem.2014.10.104 en_US
dc.subject UPLC-HILIC en_US
dc.subject Di-, tri- and tetrapeptides en_US
dc.subject retention time prediction en_US
dc.subject amino acid coefficients en_US
dc.title Improved short peptide identification using HILIC-MS/MS: retention time prediction model based on the impact of amino acid position in the peptide sequence en_US
dc.type info:eu-repo/semantics/article en_US
dc.type.supercollection all_ul_research en_US
dc.type.supercollection ul_published_reviewed en_US
dc.date.updated 2017-04-20T16:24:20Z
dc.description.version ACCEPTED
dc.identifier.doi 10.1016/j.foodchem.2014.10.104
dc.contributor.sponsor EI en_US
dc.relation.projectid TC2013-0001 en_US
dc.rights.accessrights info:eu-repo/semantics/openAccess en_US
dc.internal.rssid 1579140
dc.internal.copyrightchecked Yes
dc.identifier.journaltitle Food Chemistry
dc.description.status peer-reviewed


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