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

Blood as connective tissue potentially contains evidence of all processes occurring within the organism, at least in trace amounts (Petricoin et al., 2006) [1]. Because of their small size, peptides penetrate cell membranes and epithelial barriers more freely than proteins. Among the peptides found...

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Main Authors: Georgij Arapidi, Maria Osetrova, Olga Ivanova, Ivan Butenko, Tatjana Saveleva, Polina Pavlovich, Nikolay Anikanov, Vadim Ivanov, Vadim Govorun
Format: Article
Language:English
Published: Elsevier 2018-06-01
Series:Data in Brief
Online Access:http://www.sciencedirect.com/science/article/pii/S235234091830369X
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author Georgij Arapidi
Maria Osetrova
Olga Ivanova
Ivan Butenko
Tatjana Saveleva
Polina Pavlovich
Nikolay Anikanov
Vadim Ivanov
Vadim Govorun
spellingShingle Georgij Arapidi
Maria Osetrova
Olga Ivanova
Ivan Butenko
Tatjana Saveleva
Polina Pavlovich
Nikolay Anikanov
Vadim Ivanov
Vadim Govorun
Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents
Data in Brief
author_facet Georgij Arapidi
Maria Osetrova
Olga Ivanova
Ivan Butenko
Tatjana Saveleva
Polina Pavlovich
Nikolay Anikanov
Vadim Ivanov
Vadim Govorun
author_sort Georgij Arapidi
title Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents
title_short Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents
title_full Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents
title_fullStr Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents
title_full_unstemmed Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents
title_sort peptidomics dataset: blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents
publisher Elsevier
series Data in Brief
issn 2352-3409
publishDate 2018-06-01
description Blood as connective tissue potentially contains evidence of all processes occurring within the organism, at least in trace amounts (Petricoin et al., 2006) [1]. 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.
url http://www.sciencedirect.com/science/article/pii/S235234091830369X
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spelling doaj-53be858233c14a40b3426079d75b02592020-11-25T01:12:13ZengElsevierData in Brief2352-34092018-06-011812041211Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbentsGeorgij Arapidi0Maria Osetrova1Olga Ivanova2Ivan Butenko3Tatjana Saveleva4Polina Pavlovich5Nikolay Anikanov6Vadim Ivanov7Vadim Govorun8Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian Federation; Moscow Institute of Physics and Technology (State University), Institutskii Per. 9, Moscow Region, Dolgoprudny 141700, Russian Federation; Federal Research and Clinical Center of Physical Chemical Medicine of the Federal Medical and Biological Agency of the Russian Federation, Malaya Pirogovskaya 1a, Moscow 119435, Russian Federation; Corresponding author at: Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian Federation.Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian Federation; Moscow Institute of Physics and Technology (State University), Institutskii Per. 9, Moscow Region, Dolgoprudny 141700, Russian FederationShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian FederationMoscow Institute of Physics and Technology (State University), Institutskii Per. 9, Moscow Region, Dolgoprudny 141700, Russian Federation; Federal Research and Clinical Center of Physical Chemical Medicine of the Federal Medical and Biological Agency of the Russian Federation, Malaya Pirogovskaya 1a, Moscow 119435, Russian FederationShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian Federation; Moscow Institute of Physics and Technology (State University), Institutskii Per. 9, Moscow Region, Dolgoprudny 141700, Russian FederationShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian Federation; Moscow Institute of Physics and Technology (State University), Institutskii Per. 9, Moscow Region, Dolgoprudny 141700, Russian FederationShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian Federation; Federal Research and Clinical Center of Physical Chemical Medicine of the Federal Medical and Biological Agency of the Russian Federation, Malaya Pirogovskaya 1a, Moscow 119435, Russian FederationShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian FederationShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, Moscow 117997, Russian Federation; Moscow Institute of Physics and Technology (State University), Institutskii Per. 9, Moscow Region, Dolgoprudny 141700, Russian Federation; Federal Research and Clinical Center of Physical Chemical Medicine of the Federal Medical and Biological Agency of the Russian Federation, Malaya Pirogovskaya 1a, Moscow 119435, Russian FederationBlood as connective tissue potentially contains evidence of all processes occurring within the organism, at least in trace amounts (Petricoin et al., 2006) [1]. 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.http://www.sciencedirect.com/science/article/pii/S235234091830369X