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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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posted on 2017-04-21, 10:45 authored by Solène Le Maux, Alice B. Nongonierma
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.

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Publication

Food Chemistry;173, pp. 847-854

Publisher

Elsevier

Note

peer-reviewed

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EI

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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

Language

English

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