Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents.

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Because of their small size, peptides penetrate cell membranes and epithelial barriers more freely than proteins. Among the peptides found in blood, there are both fragments of proteins secreted by various tissues and performing their function in plasma and receptor ligands: hormones, cytokines and mediators of cellular response (Anderson et al., 2002) [2]. In addition, in minor amounts, there are peptide disease markers (for example, oncomarkers) and even foreign peptides related to pathogenic organisms and infection agents. To propose an approach for detailed peptidome characterization, we carried out an LC-MS/MS analysis of blood serum and plasma samples taken from 20 healthy donors on a TripleTOF 5600+ mass-spectrometer. We prepared samples based on our previously developed method of peptide desorption from the surface of abundant blood plasma proteins followed by standard chromatographic steps (Ziganshin et al., 2011) [3]. The mass-spectrometry peptidomics data presented in this article have been deposited to the ProteomeXchange Consortium (Deutsch et al., 2017) [4] via the PRIDE partner repository with the dataset identifier PXD008141 and 10.6019/PXD008141.", "claims": [{"id": "claim-method", "statement": "We used the local false discovery rate scoring algorithm with standard experiment-wide protein grouping.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:29900295", "locator": "sections[15] \"Peptide identification\" paragraph 2", "quote": "We used the local false discovery rate scoring algorithm with standard experiment-wide protein grouping."}], "state": "complete"}, {"id": "claim-data-access", "statement": "The mass spectrometry peptidomics data have been deposited to the ProteomeXchange Consortium via the PRIDE[5]partner repository with the dataset identifierPXD008141 and 10.6019/PXD008141. 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