An EThcD-based method for discrimination of leucine and isoleucine residues in tryptic peptidesстатья

Статья опубликована в высокорейтинговом журнале

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Дата последнего поиска статьи во внешних источниках: 21 августа 2017 г.

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[1] An ethcd-based method for discrimination of leucine and isoleucine residues in tryptic peptides / S. Zhokhov, S. Kovalyov, T. Samgina, A. Lebedev // Journal of the American Society for Mass Spectrometry. — 2017. — Vol. 28, no. 8. — P. 1600–1611. An EThcD-based approach for the reliable discrimination of isomeric leucine and isoleucine residues in peptide de novo sequencing procedure has been proposed. A multistage fragmentation of peptide ions was performed with Orbitrap Elite mass spectrometer in electrospray ionization mode. At the first stage, z-ions were produced by ETD or ETcaD fragmentation of doubly or triply charged peptide precursor ions. These primary ions were further fragmented by HCD with broad-band ion isolation, and the resulting w-ions showed different mass for leucine and isoleucine residues. The procedure did not require manual isolation of specific z-ions prior to HCD stage. 43 tryptic peptides (3 to 27 residues) obtained by trypsinolysis of human serum albumin (HSA) and gp188 protein were analyzed. To demonstrate a proper solution for radical site migration problem three non-tryptic peptides were also analyzed. A total of 93 leucine and isoleucine residues have been considered and 83 of them were correctly identified. The developed approach can be a reasonable substitution for additional Edman degradation procedure which is still used in peptide sequencing for leucine and isoleucine discrimination. [ DOI ]

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